7bgj

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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...)
Current revision (07:48, 1 May 2024) (edit) (undo)
 
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'''Unreleased structure'''
 
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The entry 7bgj is ON HOLD until Paper Publication
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==C. thermophilum Pyruvate Dehydrogenase Complex Core==
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<StructureSection load='7bgj' size='340' side='right'caption='[[7bgj]], [[Resolution|resolution]] 6.90&Aring;' scene=''>
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== Structural highlights ==
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<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>
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</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>
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<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>
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</table>
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== Function ==
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[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>
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Authors: Tueting, C., Kastritis, P.L.
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==See Also==
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*[[Pyruvate dehydrogenase 3D structures|Pyruvate dehydrogenase 3D structures]]
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Description: C. thermophilum Pyruvate Dehydrogenase Complex Core
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== References ==
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[[Category: Unreleased Structures]]
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<references/>
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[[Category: Tueting, C]]
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__TOC__
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[[Category: Kastritis, P.L]]
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</StructureSection>
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[[Category: Chaetomium thermophilum var. thermophilum DSM 1495]]
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[[Category: Large Structures]]
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[[Category: Kastritis PL]]
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[[Category: Tueting C]]

Current revision

C. thermophilum Pyruvate Dehydrogenase Complex Core

PDB ID 7bgj

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