5xtc: Difference between revisions

From Proteopedia
Jump to navigation Jump to search
← Older editNewer edit →
m Protected "5xtc" [edit=sysop:move=sysop]
No edit summary
Line 12: Line 12:
== Function ==
== Function ==
[[http://www.uniprot.org/uniprot/NDUB8_HUMAN NDUB8_HUMAN]] Accessory subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I), that is believed not to be involved in catalysis. Complex I functions in the transfer of electrons from NADH to the respiratory chain. The immediate electron acceptor for the enzyme is believed to be ubiquinone.<ref>PMID:27626371</ref>  [[http://www.uniprot.org/uniprot/NDUB2_HUMAN NDUB2_HUMAN]] Accessory subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I), that is believed not to be involved in catalysis. Complex I functions in the transfer of electrons from NADH to the respiratory chain. The immediate electron acceptor for the enzyme is believed to be ubiquinone.<ref>PMID:27626371</ref>  [[http://www.uniprot.org/uniprot/Q4GRX1_HUMAN Q4GRX1_HUMAN]] Core subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I) that is believed to belong to the minimal assembly required for catalysis. Complex I functions in the transfer of electrons from NADH to the respiratory chain. The immediate electron acceptor for the enzyme is believed to be ubiquinone.[SAAS:SAAS00093760] [[http://www.uniprot.org/uniprot/NDUA1_HUMAN NDUA1_HUMAN]] Accessory subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I), that is believed not to be involved in catalysis. Complex I functions in the transfer of electrons from NADH to the respiratory chain. The immediate electron acceptor for the enzyme is believed to be ubiquinone.<ref>PMID:27626371</ref>  [[http://www.uniprot.org/uniprot/NDUB1_HUMAN NDUB1_HUMAN]] Accessory subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I) that is believed not to be involved in catalysis. Complex I functions in the transfer of electrons from NADH to the respiratory chain. The immediate electron acceptor for the enzyme is believed to be ubiquinone.<ref>PMID:27626371</ref>  [[http://www.uniprot.org/uniprot/B9EE38_HUMAN B9EE38_HUMAN]] Core subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I) that is believed to belong to the minimal assembly required for catalysis. Complex I functions in the transfer of electrons from NADH to the respiratory chain. The immediate electron acceptor for the enzyme is believed to be ubiquinone.[SAAS:SAAS00136983] [[http://www.uniprot.org/uniprot/NDUB4_HUMAN NDUB4_HUMAN]] Accessory subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I), that is believed not to be involved in catalysis. Complex I functions in the transfer of electrons from NADH to the respiratory chain. The immediate electron acceptor for the enzyme is believed to be ubiquinone.<ref>PMID:27626371</ref>  [[http://www.uniprot.org/uniprot/NDUS5_HUMAN NDUS5_HUMAN]] Accessory subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I), that is believed not to be involved in catalysis. Complex I functions in the transfer of electrons from NADH to the respiratory chain. The immediate electron acceptor for the enzyme is believed to be ubiquinone.<ref>PMID:27626371</ref>  [[http://www.uniprot.org/uniprot/NDUBB_HUMAN NDUBB_HUMAN]] Accessory subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I), that is believed not to be involved in catalysis. Complex I functions in the transfer of electrons from NADH to the respiratory chain. The immediate electron acceptor for the enzyme is believed to be ubiquinone.<ref>PMID:27626371</ref>  [[http://www.uniprot.org/uniprot/NDUAA_HUMAN NDUAA_HUMAN]] Accessory subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I), that is believed not to be involved in catalysis. Complex I functions in the transfer of electrons from NADH to the respiratory chain. The immediate electron acceptor for the enzyme is believed to be ubiquinone.<ref>PMID:27626371</ref>  [[http://www.uniprot.org/uniprot/ACPM_HUMAN ACPM_HUMAN]] Carrier of the growing fatty acid chain in fatty acid biosynthesis in mitochondria. Accessory and non-catalytic subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I), which functions in the transfer of electrons from NADH to the respiratory chain (By similarity). [[http://www.uniprot.org/uniprot/NDUB7_HUMAN NDUB7_HUMAN]] Accessory subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I), that is believed not to be involved in catalysis. Complex I functions in the transfer of electrons from NADH to the respiratory chain. The immediate electron acceptor for the enzyme is believed to be ubiquinone.<ref>PMID:27626371</ref>  [[http://www.uniprot.org/uniprot/NDUA3_HUMAN NDUA3_HUMAN]] Accessory subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I), that is believed not to be involved in catalysis. Complex I functions in the transfer of electrons from NADH to the respiratory chain. The immediate electron acceptor for the enzyme is believed to be ubiquinone.<ref>PMID:27626371</ref>  [[http://www.uniprot.org/uniprot/NDUB5_HUMAN NDUB5_HUMAN]] Accessory subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I), that is believed not to be involved in catalysis. Complex I functions in the transfer of electrons from NADH to the respiratory chain. The immediate electron acceptor for the enzyme is believed to be ubiquinone.<ref>PMID:27626371</ref>  [[http://www.uniprot.org/uniprot/NDUBA_HUMAN NDUBA_HUMAN]] Accessory subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I), that is believed not to be involved in catalysis. Complex I functions in the transfer of electrons from NADH to the respiratory chain. The immediate electron acceptor for the enzyme is believed to be ubiquinone.<ref>PMID:27626371</ref>  [[http://www.uniprot.org/uniprot/X5BVZ3_HUMAN X5BVZ3_HUMAN]] Core subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I) that is believed to belong to the minimal assembly required for catalysis. Complex I functions in the transfer of electrons from NADH to the respiratory chain. The immediate electron acceptor for the enzyme is believed to be ubiquinone.[SAAS:SAAS00061107] [[http://www.uniprot.org/uniprot/NDUC1_HUMAN NDUC1_HUMAN]] Accessory subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I), that is believed not to be involved in catalysis. Complex I functions in the transfer of electrons from NADH to the respiratory chain. The immediate electron acceptor for the enzyme is believed to be ubiquinone.<ref>PMID:27626371</ref>  [[http://www.uniprot.org/uniprot/NDUC2_HUMAN NDUC2_HUMAN]] Accessory subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I), that is believed not to be involved in catalysis. Complex I functions in the transfer of electrons from NADH to the respiratory chain. The immediate electron acceptor for the enzyme is believed to be ubiquinone.<ref>PMID:27626371</ref>  [[http://www.uniprot.org/uniprot/NDUB3_HUMAN NDUB3_HUMAN]] Accessory subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I), that is believed not to be involved in catalysis. Complex I functions in the transfer of electrons from NADH to the respiratory chain. The immediate electron acceptor for the enzyme is believed to be ubiquinone.<ref>PMID:27626371</ref>  [[http://www.uniprot.org/uniprot/NDUAB_HUMAN NDUAB_HUMAN]] Accessory subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I), that is believed not to be involved in catalysis. Complex I functions in the transfer of electrons from NADH to the respiratory chain. The immediate electron acceptor for the enzyme is believed to be ubiquinone.<ref>PMID:27626371</ref>  [[http://www.uniprot.org/uniprot/NDUB9_HUMAN NDUB9_HUMAN]] Accessory subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I), that is believed to be not involved in catalysis. Complex I functions in the transfer of electrons from NADH to the respiratory chain. The immediate electron acceptor for the enzyme is believed to be ubiquinone.<ref>PMID:27626371</ref>  [[http://www.uniprot.org/uniprot/V9JN72_HUMAN V9JN72_HUMAN]] Core subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I) that is believed to belong to the minimal assembly required for catalysis. Complex I functions in the transfer of electrons from NADH to the respiratory chain. The immediate electron acceptor for the enzyme is believed to be ubiquinone.[RuleBase:RU004419] [[http://www.uniprot.org/uniprot/NDUB6_HUMAN NDUB6_HUMAN]] Accessory subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I), that is believed not to be involved in catalysis. Complex I functions in the transfer of electrons from NADH to the respiratory chain. The immediate electron acceptor for the enzyme is believed to be ubiquinone.<ref>PMID:27626371</ref>  [[http://www.uniprot.org/uniprot/NDUAD_HUMAN NDUAD_HUMAN]] Accessory subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I), that is believed not to be involved in catalysis (PubMed:27626371). Complex I functions in the transfer of electrons from NADH to the respiratory chain. The immediate electron acceptor for the enzyme is believed to be ubiquinone (PubMed:27626371). Involved in the interferon/all-trans-retinoic acid (IFN/RA) induced cell death. This apoptotic activity is inhibited by interaction with viral IRF1. Prevents the transactivation of STAT3 target genes. May play a role in CARD15-mediated innate mucosal responses and serve to regulate intestinal epithelial cell responses to microbes (PubMed:15753091).<ref>PMID:12628925</ref> <ref>PMID:12867595</ref> <ref>PMID:15753091</ref> <ref>PMID:27626371</ref>   
[[http://www.uniprot.org/uniprot/NDUB8_HUMAN NDUB8_HUMAN]] Accessory subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I), that is believed not to be involved in catalysis. Complex I functions in the transfer of electrons from NADH to the respiratory chain. The immediate electron acceptor for the enzyme is believed to be ubiquinone.<ref>PMID:27626371</ref>  [[http://www.uniprot.org/uniprot/NDUB2_HUMAN NDUB2_HUMAN]] Accessory subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I), that is believed not to be involved in catalysis. Complex I functions in the transfer of electrons from NADH to the respiratory chain. The immediate electron acceptor for the enzyme is believed to be ubiquinone.<ref>PMID:27626371</ref>  [[http://www.uniprot.org/uniprot/Q4GRX1_HUMAN Q4GRX1_HUMAN]] Core subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I) that is believed to belong to the minimal assembly required for catalysis. Complex I functions in the transfer of electrons from NADH to the respiratory chain. The immediate electron acceptor for the enzyme is believed to be ubiquinone.[SAAS:SAAS00093760] [[http://www.uniprot.org/uniprot/NDUA1_HUMAN NDUA1_HUMAN]] Accessory subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I), that is believed not to be involved in catalysis. Complex I functions in the transfer of electrons from NADH to the respiratory chain. The immediate electron acceptor for the enzyme is believed to be ubiquinone.<ref>PMID:27626371</ref>  [[http://www.uniprot.org/uniprot/NDUB1_HUMAN NDUB1_HUMAN]] Accessory subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I) that is believed not to be involved in catalysis. Complex I functions in the transfer of electrons from NADH to the respiratory chain. The immediate electron acceptor for the enzyme is believed to be ubiquinone.<ref>PMID:27626371</ref>  [[http://www.uniprot.org/uniprot/B9EE38_HUMAN B9EE38_HUMAN]] Core subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I) that is believed to belong to the minimal assembly required for catalysis. Complex I functions in the transfer of electrons from NADH to the respiratory chain. The immediate electron acceptor for the enzyme is believed to be ubiquinone.[SAAS:SAAS00136983] [[http://www.uniprot.org/uniprot/NDUB4_HUMAN NDUB4_HUMAN]] Accessory subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I), that is believed not to be involved in catalysis. Complex I functions in the transfer of electrons from NADH to the respiratory chain. The immediate electron acceptor for the enzyme is believed to be ubiquinone.<ref>PMID:27626371</ref>  [[http://www.uniprot.org/uniprot/NDUS5_HUMAN NDUS5_HUMAN]] Accessory subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I), that is believed not to be involved in catalysis. Complex I functions in the transfer of electrons from NADH to the respiratory chain. The immediate electron acceptor for the enzyme is believed to be ubiquinone.<ref>PMID:27626371</ref>  [[http://www.uniprot.org/uniprot/NDUBB_HUMAN NDUBB_HUMAN]] Accessory subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I), that is believed not to be involved in catalysis. Complex I functions in the transfer of electrons from NADH to the respiratory chain. The immediate electron acceptor for the enzyme is believed to be ubiquinone.<ref>PMID:27626371</ref>  [[http://www.uniprot.org/uniprot/NDUAA_HUMAN NDUAA_HUMAN]] Accessory subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I), that is believed not to be involved in catalysis. Complex I functions in the transfer of electrons from NADH to the respiratory chain. The immediate electron acceptor for the enzyme is believed to be ubiquinone.<ref>PMID:27626371</ref>  [[http://www.uniprot.org/uniprot/ACPM_HUMAN ACPM_HUMAN]] Carrier of the growing fatty acid chain in fatty acid biosynthesis in mitochondria. Accessory and non-catalytic subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I), which functions in the transfer of electrons from NADH to the respiratory chain (By similarity). [[http://www.uniprot.org/uniprot/NDUB7_HUMAN NDUB7_HUMAN]] Accessory subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I), that is believed not to be involved in catalysis. Complex I functions in the transfer of electrons from NADH to the respiratory chain. The immediate electron acceptor for the enzyme is believed to be ubiquinone.<ref>PMID:27626371</ref>  [[http://www.uniprot.org/uniprot/NDUA3_HUMAN NDUA3_HUMAN]] Accessory subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I), that is believed not to be involved in catalysis. Complex I functions in the transfer of electrons from NADH to the respiratory chain. The immediate electron acceptor for the enzyme is believed to be ubiquinone.<ref>PMID:27626371</ref>  [[http://www.uniprot.org/uniprot/NDUB5_HUMAN NDUB5_HUMAN]] Accessory subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I), that is believed not to be involved in catalysis. Complex I functions in the transfer of electrons from NADH to the respiratory chain. The immediate electron acceptor for the enzyme is believed to be ubiquinone.<ref>PMID:27626371</ref>  [[http://www.uniprot.org/uniprot/NDUBA_HUMAN NDUBA_HUMAN]] Accessory subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I), that is believed not to be involved in catalysis. Complex I functions in the transfer of electrons from NADH to the respiratory chain. The immediate electron acceptor for the enzyme is believed to be ubiquinone.<ref>PMID:27626371</ref>  [[http://www.uniprot.org/uniprot/X5BVZ3_HUMAN X5BVZ3_HUMAN]] Core subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I) that is believed to belong to the minimal assembly required for catalysis. Complex I functions in the transfer of electrons from NADH to the respiratory chain. The immediate electron acceptor for the enzyme is believed to be ubiquinone.[SAAS:SAAS00061107] [[http://www.uniprot.org/uniprot/NDUC1_HUMAN NDUC1_HUMAN]] Accessory subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I), that is believed not to be involved in catalysis. Complex I functions in the transfer of electrons from NADH to the respiratory chain. The immediate electron acceptor for the enzyme is believed to be ubiquinone.<ref>PMID:27626371</ref>  [[http://www.uniprot.org/uniprot/NDUC2_HUMAN NDUC2_HUMAN]] Accessory subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I), that is believed not to be involved in catalysis. Complex I functions in the transfer of electrons from NADH to the respiratory chain. The immediate electron acceptor for the enzyme is believed to be ubiquinone.<ref>PMID:27626371</ref>  [[http://www.uniprot.org/uniprot/NDUB3_HUMAN NDUB3_HUMAN]] Accessory subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I), that is believed not to be involved in catalysis. Complex I functions in the transfer of electrons from NADH to the respiratory chain. The immediate electron acceptor for the enzyme is believed to be ubiquinone.<ref>PMID:27626371</ref>  [[http://www.uniprot.org/uniprot/NDUAB_HUMAN NDUAB_HUMAN]] Accessory subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I), that is believed not to be involved in catalysis. Complex I functions in the transfer of electrons from NADH to the respiratory chain. The immediate electron acceptor for the enzyme is believed to be ubiquinone.<ref>PMID:27626371</ref>  [[http://www.uniprot.org/uniprot/NDUB9_HUMAN NDUB9_HUMAN]] Accessory subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I), that is believed to be not involved in catalysis. Complex I functions in the transfer of electrons from NADH to the respiratory chain. The immediate electron acceptor for the enzyme is believed to be ubiquinone.<ref>PMID:27626371</ref>  [[http://www.uniprot.org/uniprot/V9JN72_HUMAN V9JN72_HUMAN]] Core subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I) that is believed to belong to the minimal assembly required for catalysis. Complex I functions in the transfer of electrons from NADH to the respiratory chain. The immediate electron acceptor for the enzyme is believed to be ubiquinone.[RuleBase:RU004419] [[http://www.uniprot.org/uniprot/NDUB6_HUMAN NDUB6_HUMAN]] Accessory subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I), that is believed not to be involved in catalysis. Complex I functions in the transfer of electrons from NADH to the respiratory chain. The immediate electron acceptor for the enzyme is believed to be ubiquinone.<ref>PMID:27626371</ref>  [[http://www.uniprot.org/uniprot/NDUAD_HUMAN NDUAD_HUMAN]] Accessory subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I), that is believed not to be involved in catalysis (PubMed:27626371). Complex I functions in the transfer of electrons from NADH to the respiratory chain. The immediate electron acceptor for the enzyme is believed to be ubiquinone (PubMed:27626371). Involved in the interferon/all-trans-retinoic acid (IFN/RA) induced cell death. This apoptotic activity is inhibited by interaction with viral IRF1. Prevents the transactivation of STAT3 target genes. May play a role in CARD15-mediated innate mucosal responses and serve to regulate intestinal epithelial cell responses to microbes (PubMed:15753091).<ref>PMID:12628925</ref> <ref>PMID:12867595</ref> <ref>PMID:15753091</ref> <ref>PMID:27626371</ref>   
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
The respiratory megacomplex represents the highest-order assembly of respiratory chain complexes, and it allows mitochondria to respond to energy-requiring conditions. To understand its architecture, we examined the human respiratory chain megacomplex-I2III2IV2 (MCI2III2IV2) with 140 subunits and a subset of associated cofactors using cryo-electron microscopy. The MCI2III2IV2 forms a circular structure with the dimeric CIII located in the center, where it is surrounded by two copies each of CI and CIV. Two cytochrome c (Cyt.c) molecules are positioned to accept electrons on the surface of the c1 state CIII dimer. Analyses indicate that CII could insert into the gaps between CI and CIV to form a closed ring, which we termed the electron transport chain supercomplex. The structure not only reveals the precise assignment of individual subunits of human CI and CIII, but also enables future in-depth analysis of the electron transport chain as a whole.
Architecture of Human Mitochondrial Respiratory Megacomplex I2III2IV2.,Guo R, Zong S, Wu M, Gu J, Yang M Cell. 2017 Sep 7;170(6):1247-1257.e12. doi: 10.1016/j.cell.2017.07.050. Epub 2017, Aug 24. PMID:28844695<ref>PMID:28844695</ref>
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 5xtc" style="background-color:#fffaf0;"></div>
== References ==
== References ==
<references/>
<references/>

Revision as of 10:56, 6 December 2017

Cryo-EM structure of human respiratory complex I transmembrane armCryo-EM structure of human respiratory complex I transmembrane arm

Structural highlights

5xtc is a 29 chain structure with sequence from Homo sapiens. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:, , ,
Activity:NADH:ubiquinone reductase (H(+)-translocating), with EC number 1.6.5.3
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Disease

[NDUA1_HUMAN] Isolated NADH-CoQ reductase deficiency. The disease is caused by mutations affecting the gene represented in this entry. [NDUBB_HUMAN] The disease is caused by mutations affecting the gene represented in this entry. The disease is caused by mutations affecting the gene represented in this entry. The disease may be caused by mutations affecting the gene represented in this entry. [NDUAA_HUMAN] Leigh syndrome with leukodystrophy. The disease is caused by mutations affecting the gene represented in this entry. [NDUB3_HUMAN] Isolated NADH-CoQ reductase deficiency. The disease is caused by mutations affecting the gene represented in this entry. [NDUAB_HUMAN] Isolated NADH-CoQ reductase deficiency. The disease is caused by mutations affecting the gene represented in this entry. [NDUB9_HUMAN] Isolated NADH-CoQ reductase deficiency. [NDUAD_HUMAN] Papillary or follicular thyroid carcinoma. Disease susceptibility is associated with variations affecting the gene represented in this entry. Defects in NDUFA13 are a cause of a mitochondrial complex I deficiency characterized by early onset hypotonia, dyskinesia and sensorial deficiencies, as well as a severe optic neuropathy.[1]

Function

[NDUB8_HUMAN] Accessory subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I), that is believed not to be involved in catalysis. Complex I functions in the transfer of electrons from NADH to the respiratory chain. The immediate electron acceptor for the enzyme is believed to be ubiquinone.[2] [NDUB2_HUMAN] Accessory subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I), that is believed not to be involved in catalysis. Complex I functions in the transfer of electrons from NADH to the respiratory chain. The immediate electron acceptor for the enzyme is believed to be ubiquinone.[3] [Q4GRX1_HUMAN] Core subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I) that is believed to belong to the minimal assembly required for catalysis. Complex I functions in the transfer of electrons from NADH to the respiratory chain. The immediate electron acceptor for the enzyme is believed to be ubiquinone.[SAAS:SAAS00093760] [NDUA1_HUMAN] Accessory subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I), that is believed not to be involved in catalysis. Complex I functions in the transfer of electrons from NADH to the respiratory chain. The immediate electron acceptor for the enzyme is believed to be ubiquinone.[4] [NDUB1_HUMAN] Accessory subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I) that is believed not to be involved in catalysis. Complex I functions in the transfer of electrons from NADH to the respiratory chain. The immediate electron acceptor for the enzyme is believed to be ubiquinone.[5] [B9EE38_HUMAN] Core subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I) that is believed to belong to the minimal assembly required for catalysis. Complex I functions in the transfer of electrons from NADH to the respiratory chain. The immediate electron acceptor for the enzyme is believed to be ubiquinone.[SAAS:SAAS00136983] [NDUB4_HUMAN] Accessory subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I), that is believed not to be involved in catalysis. Complex I functions in the transfer of electrons from NADH to the respiratory chain. The immediate electron acceptor for the enzyme is believed to be ubiquinone.[6] [NDUS5_HUMAN] Accessory subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I), that is believed not to be involved in catalysis. Complex I functions in the transfer of electrons from NADH to the respiratory chain. The immediate electron acceptor for the enzyme is believed to be ubiquinone.[7] [NDUBB_HUMAN] Accessory subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I), that is believed not to be involved in catalysis. Complex I functions in the transfer of electrons from NADH to the respiratory chain. The immediate electron acceptor for the enzyme is believed to be ubiquinone.[8] [NDUAA_HUMAN] Accessory subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I), that is believed not to be involved in catalysis. Complex I functions in the transfer of electrons from NADH to the respiratory chain. The immediate electron acceptor for the enzyme is believed to be ubiquinone.[9] [ACPM_HUMAN] Carrier of the growing fatty acid chain in fatty acid biosynthesis in mitochondria. Accessory and non-catalytic subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I), which functions in the transfer of electrons from NADH to the respiratory chain (By similarity). [NDUB7_HUMAN] Accessory subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I), that is believed not to be involved in catalysis. Complex I functions in the transfer of electrons from NADH to the respiratory chain. The immediate electron acceptor for the enzyme is believed to be ubiquinone.[10] [NDUA3_HUMAN] Accessory subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I), that is believed not to be involved in catalysis. Complex I functions in the transfer of electrons from NADH to the respiratory chain. The immediate electron acceptor for the enzyme is believed to be ubiquinone.[11] [NDUB5_HUMAN] Accessory subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I), that is believed not to be involved in catalysis. Complex I functions in the transfer of electrons from NADH to the respiratory chain. The immediate electron acceptor for the enzyme is believed to be ubiquinone.[12] [NDUBA_HUMAN] Accessory subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I), that is believed not to be involved in catalysis. Complex I functions in the transfer of electrons from NADH to the respiratory chain. The immediate electron acceptor for the enzyme is believed to be ubiquinone.[13] [X5BVZ3_HUMAN] Core subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I) that is believed to belong to the minimal assembly required for catalysis. Complex I functions in the transfer of electrons from NADH to the respiratory chain. The immediate electron acceptor for the enzyme is believed to be ubiquinone.[SAAS:SAAS00061107] [NDUC1_HUMAN] Accessory subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I), that is believed not to be involved in catalysis. Complex I functions in the transfer of electrons from NADH to the respiratory chain. The immediate electron acceptor for the enzyme is believed to be ubiquinone.[14] [NDUC2_HUMAN] Accessory subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I), that is believed not to be involved in catalysis. Complex I functions in the transfer of electrons from NADH to the respiratory chain. The immediate electron acceptor for the enzyme is believed to be ubiquinone.[15] [NDUB3_HUMAN] Accessory subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I), that is believed not to be involved in catalysis. Complex I functions in the transfer of electrons from NADH to the respiratory chain. The immediate electron acceptor for the enzyme is believed to be ubiquinone.[16] [NDUAB_HUMAN] Accessory subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I), that is believed not to be involved in catalysis. Complex I functions in the transfer of electrons from NADH to the respiratory chain. The immediate electron acceptor for the enzyme is believed to be ubiquinone.[17] [NDUB9_HUMAN] Accessory subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I), that is believed to be not involved in catalysis. Complex I functions in the transfer of electrons from NADH to the respiratory chain. The immediate electron acceptor for the enzyme is believed to be ubiquinone.[18] [V9JN72_HUMAN] Core subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I) that is believed to belong to the minimal assembly required for catalysis. Complex I functions in the transfer of electrons from NADH to the respiratory chain. The immediate electron acceptor for the enzyme is believed to be ubiquinone.[RuleBase:RU004419] [NDUB6_HUMAN] Accessory subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I), that is believed not to be involved in catalysis. Complex I functions in the transfer of electrons from NADH to the respiratory chain. The immediate electron acceptor for the enzyme is believed to be ubiquinone.[19] [NDUAD_HUMAN] Accessory subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I), that is believed not to be involved in catalysis (PubMed:27626371). Complex I functions in the transfer of electrons from NADH to the respiratory chain. The immediate electron acceptor for the enzyme is believed to be ubiquinone (PubMed:27626371). Involved in the interferon/all-trans-retinoic acid (IFN/RA) induced cell death. This apoptotic activity is inhibited by interaction with viral IRF1. Prevents the transactivation of STAT3 target genes. May play a role in CARD15-mediated innate mucosal responses and serve to regulate intestinal epithelial cell responses to microbes (PubMed:15753091).[20] [21] [22] [23]

Publication Abstract from PubMed

The respiratory megacomplex represents the highest-order assembly of respiratory chain complexes, and it allows mitochondria to respond to energy-requiring conditions. To understand its architecture, we examined the human respiratory chain megacomplex-I2III2IV2 (MCI2III2IV2) with 140 subunits and a subset of associated cofactors using cryo-electron microscopy. The MCI2III2IV2 forms a circular structure with the dimeric CIII located in the center, where it is surrounded by two copies each of CI and CIV. Two cytochrome c (Cyt.c) molecules are positioned to accept electrons on the surface of the c1 state CIII dimer. Analyses indicate that CII could insert into the gaps between CI and CIV to form a closed ring, which we termed the electron transport chain supercomplex. The structure not only reveals the precise assignment of individual subunits of human CI and CIII, but also enables future in-depth analysis of the electron transport chain as a whole.

Architecture of Human Mitochondrial Respiratory Megacomplex I2III2IV2.,Guo R, Zong S, Wu M, Gu J, Yang M Cell. 2017 Sep 7;170(6):1247-1257.e12. doi: 10.1016/j.cell.2017.07.050. Epub 2017, Aug 24. PMID:28844695[24]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

  1. ↑ Angebault C, Charif M, Guegen N, Piro-Megy C, Mousson de Camaret B, Procaccio V, Guichet PO, Hebrard M, Manes G, Leboucq N, Rivier F, Hamel CP, Lenaers G, Roubertie A. Mutation in NDUFA13/GRIM19 leads to early onset hypotonia, dyskinesia and sensorial deficiencies, and mitochondrial complex I instability. Hum Mol Genet. 2015 Jul 15;24(14):3948-55. doi: 10.1093/hmg/ddv133. Epub 2015 Apr, 21. PMID:25901006 doi:http://dx.doi.org/10.1093/hmg/ddv133
  2. ↑ Stroud DA, Surgenor EE, Formosa LE, Reljic B, Frazier AE, Dibley MG, Osellame LD, Stait T, Beilharz TH, Thorburn DR, Salim A, Ryan MT. Accessory subunits are integral for assembly and function of human mitochondrial complex I. Nature. 2016 Oct 6;538(7623):123-126. doi: 10.1038/nature19754. Epub 2016 Sep 14. PMID:27626371 doi:http://dx.doi.org/10.1038/nature19754
  3. ↑ Stroud DA, Surgenor EE, Formosa LE, Reljic B, Frazier AE, Dibley MG, Osellame LD, Stait T, Beilharz TH, Thorburn DR, Salim A, Ryan MT. Accessory subunits are integral for assembly and function of human mitochondrial complex I. Nature. 2016 Oct 6;538(7623):123-126. doi: 10.1038/nature19754. Epub 2016 Sep 14. PMID:27626371 doi:http://dx.doi.org/10.1038/nature19754
  4. ↑ Stroud DA, Surgenor EE, Formosa LE, Reljic B, Frazier AE, Dibley MG, Osellame LD, Stait T, Beilharz TH, Thorburn DR, Salim A, Ryan MT. Accessory subunits are integral for assembly and function of human mitochondrial complex I. Nature. 2016 Oct 6;538(7623):123-126. doi: 10.1038/nature19754. Epub 2016 Sep 14. PMID:27626371 doi:http://dx.doi.org/10.1038/nature19754
  5. ↑ Stroud DA, Surgenor EE, Formosa LE, Reljic B, Frazier AE, Dibley MG, Osellame LD, Stait T, Beilharz TH, Thorburn DR, Salim A, Ryan MT. Accessory subunits are integral for assembly and function of human mitochondrial complex I. Nature. 2016 Oct 6;538(7623):123-126. doi: 10.1038/nature19754. Epub 2016 Sep 14. PMID:27626371 doi:http://dx.doi.org/10.1038/nature19754
  6. ↑ Stroud DA, Surgenor EE, Formosa LE, Reljic B, Frazier AE, Dibley MG, Osellame LD, Stait T, Beilharz TH, Thorburn DR, Salim A, Ryan MT. Accessory subunits are integral for assembly and function of human mitochondrial complex I. Nature. 2016 Oct 6;538(7623):123-126. doi: 10.1038/nature19754. Epub 2016 Sep 14. PMID:27626371 doi:http://dx.doi.org/10.1038/nature19754
  7. ↑ Stroud DA, Surgenor EE, Formosa LE, Reljic B, Frazier AE, Dibley MG, Osellame LD, Stait T, Beilharz TH, Thorburn DR, Salim A, Ryan MT. Accessory subunits are integral for assembly and function of human mitochondrial complex I. Nature. 2016 Oct 6;538(7623):123-126. doi: 10.1038/nature19754. Epub 2016 Sep 14. PMID:27626371 doi:http://dx.doi.org/10.1038/nature19754
  8. ↑ Stroud DA, Surgenor EE, Formosa LE, Reljic B, Frazier AE, Dibley MG, Osellame LD, Stait T, Beilharz TH, Thorburn DR, Salim A, Ryan MT. Accessory subunits are integral for assembly and function of human mitochondrial complex I. Nature. 2016 Oct 6;538(7623):123-126. doi: 10.1038/nature19754. Epub 2016 Sep 14. PMID:27626371 doi:http://dx.doi.org/10.1038/nature19754
  9. ↑ Stroud DA, Surgenor EE, Formosa LE, Reljic B, Frazier AE, Dibley MG, Osellame LD, Stait T, Beilharz TH, Thorburn DR, Salim A, Ryan MT. Accessory subunits are integral for assembly and function of human mitochondrial complex I. Nature. 2016 Oct 6;538(7623):123-126. doi: 10.1038/nature19754. Epub 2016 Sep 14. PMID:27626371 doi:http://dx.doi.org/10.1038/nature19754
  10. ↑ Stroud DA, Surgenor EE, Formosa LE, Reljic B, Frazier AE, Dibley MG, Osellame LD, Stait T, Beilharz TH, Thorburn DR, Salim A, Ryan MT. Accessory subunits are integral for assembly and function of human mitochondrial complex I. Nature. 2016 Oct 6;538(7623):123-126. doi: 10.1038/nature19754. Epub 2016 Sep 14. PMID:27626371 doi:http://dx.doi.org/10.1038/nature19754
  11. ↑ Stroud DA, Surgenor EE, Formosa LE, Reljic B, Frazier AE, Dibley MG, Osellame LD, Stait T, Beilharz TH, Thorburn DR, Salim A, Ryan MT. Accessory subunits are integral for assembly and function of human mitochondrial complex I. Nature. 2016 Oct 6;538(7623):123-126. doi: 10.1038/nature19754. Epub 2016 Sep 14. PMID:27626371 doi:http://dx.doi.org/10.1038/nature19754
  12. ↑ Stroud DA, Surgenor EE, Formosa LE, Reljic B, Frazier AE, Dibley MG, Osellame LD, Stait T, Beilharz TH, Thorburn DR, Salim A, Ryan MT. Accessory subunits are integral for assembly and function of human mitochondrial complex I. Nature. 2016 Oct 6;538(7623):123-126. doi: 10.1038/nature19754. Epub 2016 Sep 14. PMID:27626371 doi:http://dx.doi.org/10.1038/nature19754
  13. ↑ Stroud DA, Surgenor EE, Formosa LE, Reljic B, Frazier AE, Dibley MG, Osellame LD, Stait T, Beilharz TH, Thorburn DR, Salim A, Ryan MT. Accessory subunits are integral for assembly and function of human mitochondrial complex I. Nature. 2016 Oct 6;538(7623):123-126. doi: 10.1038/nature19754. Epub 2016 Sep 14. PMID:27626371 doi:http://dx.doi.org/10.1038/nature19754
  14. ↑ Stroud DA, Surgenor EE, Formosa LE, Reljic B, Frazier AE, Dibley MG, Osellame LD, Stait T, Beilharz TH, Thorburn DR, Salim A, Ryan MT. Accessory subunits are integral for assembly and function of human mitochondrial complex I. Nature. 2016 Oct 6;538(7623):123-126. doi: 10.1038/nature19754. Epub 2016 Sep 14. PMID:27626371 doi:http://dx.doi.org/10.1038/nature19754
  15. ↑ Stroud DA, Surgenor EE, Formosa LE, Reljic B, Frazier AE, Dibley MG, Osellame LD, Stait T, Beilharz TH, Thorburn DR, Salim A, Ryan MT. Accessory subunits are integral for assembly and function of human mitochondrial complex I. Nature. 2016 Oct 6;538(7623):123-126. doi: 10.1038/nature19754. Epub 2016 Sep 14. PMID:27626371 doi:http://dx.doi.org/10.1038/nature19754
  16. ↑ Stroud DA, Surgenor EE, Formosa LE, Reljic B, Frazier AE, Dibley MG, Osellame LD, Stait T, Beilharz TH, Thorburn DR, Salim A, Ryan MT. Accessory subunits are integral for assembly and function of human mitochondrial complex I. Nature. 2016 Oct 6;538(7623):123-126. doi: 10.1038/nature19754. Epub 2016 Sep 14. PMID:27626371 doi:http://dx.doi.org/10.1038/nature19754
  17. ↑ Stroud DA, Surgenor EE, Formosa LE, Reljic B, Frazier AE, Dibley MG, Osellame LD, Stait T, Beilharz TH, Thorburn DR, Salim A, Ryan MT. Accessory subunits are integral for assembly and function of human mitochondrial complex I. Nature. 2016 Oct 6;538(7623):123-126. doi: 10.1038/nature19754. Epub 2016 Sep 14. PMID:27626371 doi:http://dx.doi.org/10.1038/nature19754
  18. ↑ Stroud DA, Surgenor EE, Formosa LE, Reljic B, Frazier AE, Dibley MG, Osellame LD, Stait T, Beilharz TH, Thorburn DR, Salim A, Ryan MT. Accessory subunits are integral for assembly and function of human mitochondrial complex I. Nature. 2016 Oct 6;538(7623):123-126. doi: 10.1038/nature19754. Epub 2016 Sep 14. PMID:27626371 doi:http://dx.doi.org/10.1038/nature19754
  19. ↑ Stroud DA, Surgenor EE, Formosa LE, Reljic B, Frazier AE, Dibley MG, Osellame LD, Stait T, Beilharz TH, Thorburn DR, Salim A, Ryan MT. Accessory subunits are integral for assembly and function of human mitochondrial complex I. Nature. 2016 Oct 6;538(7623):123-126. doi: 10.1038/nature19754. Epub 2016 Sep 14. PMID:27626371 doi:http://dx.doi.org/10.1038/nature19754
  20. ↑ Lufei C, Ma J, Huang G, Zhang T, Novotny-Diermayr V, Ong CT, Cao X. GRIM-19, a death-regulatory gene product, suppresses Stat3 activity via functional interaction. EMBO J. 2003 Mar 17;22(6):1325-35. PMID:12628925 doi:http://dx.doi.org/10.1093/emboj/cdg135
  21. ↑ Zhang J, Yang J, Roy SK, Tininini S, Hu J, Bromberg JF, Poli V, Stark GR, Kalvakolanu DV. The cell death regulator GRIM-19 is an inhibitor of signal transducer and activator of transcription 3. Proc Natl Acad Sci U S A. 2003 Aug 5;100(16):9342-7. Epub 2003 Jul 16. PMID:12867595 doi:http://dx.doi.org/10.1073/pnas.1633516100
  22. ↑ Barnich N, Hisamatsu T, Aguirre JE, Xavier R, Reinecker HC, Podolsky DK. GRIM-19 interacts with nucleotide oligomerization domain 2 and serves as downstream effector of anti-bacterial function in intestinal epithelial cells. J Biol Chem. 2005 May 13;280(19):19021-6. Epub 2005 Mar 7. PMID:15753091 doi:http://dx.doi.org/10.1074/jbc.M413776200
  23. ↑ Stroud DA, Surgenor EE, Formosa LE, Reljic B, Frazier AE, Dibley MG, Osellame LD, Stait T, Beilharz TH, Thorburn DR, Salim A, Ryan MT. Accessory subunits are integral for assembly and function of human mitochondrial complex I. Nature. 2016 Oct 6;538(7623):123-126. doi: 10.1038/nature19754. Epub 2016 Sep 14. PMID:27626371 doi:http://dx.doi.org/10.1038/nature19754
  24. ↑ Guo R, Zong S, Wu M, Gu J, Yang M. Architecture of Human Mitochondrial Respiratory Megacomplex I2III2IV2. Cell. 2017 Sep 7;170(6):1247-1257.e12. doi: 10.1016/j.cell.2017.07.050. Epub 2017, Aug 24. PMID:28844695 doi:http://dx.doi.org/10.1016/j.cell.2017.07.050

5xtc, resolution 3.70Å

Drag the structure with the mouse to rotate

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA
Retrieved from "https://proteopedia.openfox.io/wiki/index.php?title=5xtc&oldid=2830839"