7bgj: Difference between revisions

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New page: '''Unreleased structure''' The entry 7bgj is ON HOLD until Paper Publication Authors: Tueting, C., Kastritis, P.L. Description: C. thermophilum Pyruvate Dehydrogenase Complex Core [[Ca...
 
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'''Unreleased structure'''


The entry 7bgj is ON HOLD  until Paper Publication
==C. thermophilum Pyruvate Dehydrogenase Complex Core==
<StructureSection load='7bgj' size='340' side='right'caption='[[7bgj]], [[Resolution|resolution]] 6.90&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[7bgj]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Chaetomium_thermophilum_var._thermophilum_DSM_1495 Chaetomium thermophilum var. thermophilum DSM 1495]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7BGJ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7BGJ FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Electron Microscopy, [[Resolution|Resolution]] 6.9&#8491;</td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=7bgj FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7bgj OCA], [https://pdbe.org/7bgj PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7bgj RCSB], [https://www.ebi.ac.uk/pdbsum/7bgj PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7bgj ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/ODP2_CHATD ODP2_CHATD] The 10-megadalton pyruvate dehydrogenase complex contains multiple copies of three enzymatic components: pyruvate dehydrogenase (E1), dihydrolipoamide acetyltransferase (E2) and lipoamide dehydrogenase (E3) and catalyzes the overall oxidative decarboxylation of pyruvate to form acetyl-CoA and CO(2) (PubMed:33567276, PubMed:34836937, PubMed:35093201). Within the complex, pyruvate and thiamine pyrophosphate (TPP or vitamin B1) are bound by pyruvate dehydrogenase E1 subunits alpha and beta and pyruvate is decarboxylated leading to the 2-carbon hydrohyethyl bound to TPP. The E2 component contains covalently-bound lipoyl cofactors and transfers the hydroxyethyl group from TPP to an oxidized form of covalently bound lipoamide, and the resulting acetyl group is then transferred to free coenzyme A to form acetyl-CoA and reduced dihydrolipoamide-E2. Finally, the flavoprotein dihydrolipoamide dehydrogenase (E3) re-oxidizes the lipoyl group of dihydrolipoamide-E2 to form lipoamide-E2 and NADH. A fourth subunit, E3BP, is responsible for tethering E3 in proximity to the core, forming the entire metabolon (Probable).<ref>PMID:33567276</ref> <ref>PMID:34836937</ref> <ref>PMID:35093201</ref> <ref>PMID:33567276</ref>


Authors: Tueting, C., Kastritis, P.L.
==See Also==
 
*[[Pyruvate dehydrogenase 3D structures|Pyruvate dehydrogenase 3D structures]]
Description: C. thermophilum Pyruvate Dehydrogenase Complex Core
== References ==
[[Category: Unreleased Structures]]
<references/>
[[Category: Tueting, C]]
__TOC__
[[Category: Kastritis, P.L]]
</StructureSection>
[[Category: Chaetomium thermophilum var. thermophilum DSM 1495]]
[[Category: Large Structures]]
[[Category: Kastritis PL]]
[[Category: Tueting C]]

Latest revision as of 10:48, 1 May 2024

C. thermophilum Pyruvate Dehydrogenase Complex CoreC. thermophilum Pyruvate Dehydrogenase Complex Core

Structural highlights

7bgj is a 1 chain structure with sequence from Chaetomium thermophilum var. thermophilum DSM 1495. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:Electron Microscopy, Resolution 6.9Å
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

ODP2_CHATD The 10-megadalton pyruvate dehydrogenase complex contains multiple copies of three enzymatic components: pyruvate dehydrogenase (E1), dihydrolipoamide acetyltransferase (E2) and lipoamide dehydrogenase (E3) and catalyzes the overall oxidative decarboxylation of pyruvate to form acetyl-CoA and CO(2) (PubMed:33567276, PubMed:34836937, PubMed:35093201). Within the complex, pyruvate and thiamine pyrophosphate (TPP or vitamin B1) are bound by pyruvate dehydrogenase E1 subunits alpha and beta and pyruvate is decarboxylated leading to the 2-carbon hydrohyethyl bound to TPP. The E2 component contains covalently-bound lipoyl cofactors and transfers the hydroxyethyl group from TPP to an oxidized form of covalently bound lipoamide, and the resulting acetyl group is then transferred to free coenzyme A to form acetyl-CoA and reduced dihydrolipoamide-E2. Finally, the flavoprotein dihydrolipoamide dehydrogenase (E3) re-oxidizes the lipoyl group of dihydrolipoamide-E2 to form lipoamide-E2 and NADH. A fourth subunit, E3BP, is responsible for tethering E3 in proximity to the core, forming the entire metabolon (Probable).[1] [2] [3] [4]

See Also

References

  1. ↑ Kyrilis FL, Semchonok DA, Skalidis I, Tüting C, Hamdi F, O'Reilly FJ, Rappsilber J, Kastritis PL. Integrative structure of a 10-megadalton eukaryotic pyruvate dehydrogenase complex from native cell extracts. Cell Rep. 2021 Feb 9;34(6):108727. PMID:33567276 doi:10.1016/j.celrep.2021.108727
  2. ↑ Tuting C, Kyrilis FL, Muller J, Sorokina M, Skalidis I, Hamdi F, Sadian Y, Kastritis PL. Cryo-EM snapshots of a native lysate provide structural insights into a metabolon-embedded transacetylase reaction. Nat Commun. 2021 Nov 26;12(1):6933. doi: 10.1038/s41467-021-27287-4. PMID:34836937 doi:http://dx.doi.org/10.1038/s41467-021-27287-4
  3. ↑ Skalidis I, Kyrilis FL, Tuting C, Hamdi F, Chojnowski G, Kastritis PL. Cryo-EM and artificial intelligence visualize endogenous protein community members. Structure. 2022 Jan 19. pii: S0969-2126(22)00001-6. doi:, 10.1016/j.str.2022.01.001. PMID:35093201 doi:http://dx.doi.org/10.1016/j.str.2022.01.001
  4. ↑ Kyrilis FL, Semchonok DA, Skalidis I, Tüting C, Hamdi F, O'Reilly FJ, Rappsilber J, Kastritis PL. Integrative structure of a 10-megadalton eukaryotic pyruvate dehydrogenase complex from native cell extracts. Cell Rep. 2021 Feb 9;34(6):108727. PMID:33567276 doi:10.1016/j.celrep.2021.108727

7bgj, resolution 6.90Å

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