8d9x: Difference between revisions

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'''Unreleased structure'''


The entry 8d9x is ON HOLD
==Cryo-EM structure of human DELE1 in oligomeric form==
 
<StructureSection load='8d9x' size='340' side='right'caption='[[8d9x]], [[Resolution|resolution]] 3.80&Aring;' scene=''>
Authors: Yang, J., Lander, G.C.
== Structural highlights ==
 
<table><tr><td colspan='2'>[[8d9x]] is a 8 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=8D9X OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=8D9X FirstGlance]. <br>
Description: Cryo-EM structure of human DELE1 in oligomeric form
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Electron Microscopy, [[Resolution|Resolution]] 3.8&#8491;</td></tr>
[[Category: Unreleased Structures]]
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=8d9x FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8d9x OCA], [https://pdbe.org/8d9x PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8d9x RCSB], [https://www.ebi.ac.uk/pdbsum/8d9x PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8d9x ProSAT]</span></td></tr>
[[Category: Lander, G.C]]
</table>
[[Category: Yang, J]]
== Function ==
[https://www.uniprot.org/uniprot/DELE1_HUMAN DELE1_HUMAN] Key activator of the integrated stress response (ISR) following mitochondrial stress (PubMed:32132706, PubMed:32132707). In response to mitochondrial stress, cleaved by the protease OMA1, generating the DAP3-binding cell death enhancer 1 short form (DELE1(S) or S-DELE1), which translocates to the cytosol and activates EIF2AK1/HRI to trigger the ISR (PubMed:32132706, PubMed:32132707). Essential for the induction of death receptor-mediated apoptosis through the regulation of caspase activation (PubMed:20563667).<ref>PMID:20563667</ref> <ref>PMID:32132706</ref> <ref>PMID:32132707</ref>  Protein kinase activator generated by protein cleavage in response to mitochondrial stress, which accumulates in the cytosol and specifically binds to and activates the protein kinase activity of EIF2AK1/HRI (PubMed:32132706, PubMed:32132707). It thereby activates the integrated stress response (ISR): EIF2AK1/HRI activation promotes eIF-2-alpha (EIF2S1) phosphorylation, leading to a decrease in global protein synthesis and the induction of selected genes, including the transcription factor ATF4, the master transcriptional regulator of the ISR (PubMed:32132706, PubMed:32132707).<ref>PMID:32132706</ref> <ref>PMID:32132707</ref> [https://www.uniprot.org/uniprot/A0A376KDN7_ECOLX A0A376KDN7_ECOLX] Part of the ABC transporter complex MalEFGK involved in maltose/maltodextrin import. Binds maltose and higher maltodextrins.[RuleBase:RU365005]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Homo sapiens]]
[[Category: Large Structures]]
[[Category: Lander GC]]
[[Category: Yang J]]

Latest revision as of 09:58, 9 August 2023

Cryo-EM structure of human DELE1 in oligomeric formCryo-EM structure of human DELE1 in oligomeric form

Structural highlights

8d9x is a 8 chain structure with sequence from Homo sapiens. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:Electron Microscopy, Resolution 3.8Å
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

DELE1_HUMAN Key activator of the integrated stress response (ISR) following mitochondrial stress (PubMed:32132706, PubMed:32132707). In response to mitochondrial stress, cleaved by the protease OMA1, generating the DAP3-binding cell death enhancer 1 short form (DELE1(S) or S-DELE1), which translocates to the cytosol and activates EIF2AK1/HRI to trigger the ISR (PubMed:32132706, PubMed:32132707). Essential for the induction of death receptor-mediated apoptosis through the regulation of caspase activation (PubMed:20563667).[1] [2] [3] Protein kinase activator generated by protein cleavage in response to mitochondrial stress, which accumulates in the cytosol and specifically binds to and activates the protein kinase activity of EIF2AK1/HRI (PubMed:32132706, PubMed:32132707). It thereby activates the integrated stress response (ISR): EIF2AK1/HRI activation promotes eIF-2-alpha (EIF2S1) phosphorylation, leading to a decrease in global protein synthesis and the induction of selected genes, including the transcription factor ATF4, the master transcriptional regulator of the ISR (PubMed:32132706, PubMed:32132707).[4] [5] A0A376KDN7_ECOLX Part of the ABC transporter complex MalEFGK involved in maltose/maltodextrin import. Binds maltose and higher maltodextrins.[RuleBase:RU365005]

References

  1. Harada T, Iwai A, Miyazaki T. Identification of DELE, a novel DAP3-binding protein which is crucial for death receptor-mediated apoptosis induction. Apoptosis. 2010 Oct;15(10):1247-55. PMID:20563667 doi:10.1007/s10495-010-0519-3
  2. Fessler E, Eckl EM, Schmitt S, Mancilla IA, Meyer-Bender MF, Hanf M, Philippou-Massier J, Krebs S, Zischka H, Jae LT. A pathway coordinated by DELE1 relays mitochondrial stress to the cytosol. Nature. 2020 Mar;579(7799):433-437. PMID:32132706 doi:10.1038/s41586-020-2076-4
  3. Guo X, Aviles G, Liu Y, Tian R, Unger BA, Lin YT, Wiita AP, Xu K, Correia MA, Kampmann M. Mitochondrial stress is relayed to the cytosol by an OMA1-DELE1-HRI pathway. Nature. 2020 Mar;579(7799):427-432. PMID:32132707 doi:10.1038/s41586-020-2078-2
  4. Fessler E, Eckl EM, Schmitt S, Mancilla IA, Meyer-Bender MF, Hanf M, Philippou-Massier J, Krebs S, Zischka H, Jae LT. A pathway coordinated by DELE1 relays mitochondrial stress to the cytosol. Nature. 2020 Mar;579(7799):433-437. PMID:32132706 doi:10.1038/s41586-020-2076-4
  5. Guo X, Aviles G, Liu Y, Tian R, Unger BA, Lin YT, Wiita AP, Xu K, Correia MA, Kampmann M. Mitochondrial stress is relayed to the cytosol by an OMA1-DELE1-HRI pathway. Nature. 2020 Mar;579(7799):427-432. PMID:32132707 doi:10.1038/s41586-020-2078-2

8d9x, resolution 3.80Å

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