7q5r: Difference between revisions

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<StructureSection load='7q5r' size='340' side='right'caption='[[7q5r]], [[Resolution|resolution]] 3.84&Aring;' scene=''>
<StructureSection load='7q5r' size='340' side='right'caption='[[7q5r]], [[Resolution|resolution]] 3.84&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[7q5r]] is a 60 chain structure with sequence from [https://en.wikipedia.org/wiki/Chaetomium_thermophilum_(strain_dsm_1495_/_cbs_144.50_/_imi_039719) Chaetomium thermophilum (strain dsm 1495 / cbs 144.50 / imi 039719)]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7Q5R OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7Q5R FirstGlance]. <br>
<table><tr><td colspan='2'>[[7q5r]] is a 60 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=7Q5R OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7Q5R FirstGlance]. <br>
</td></tr><tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Dihydrolipoyllysine-residue_acetyltransferase Dihydrolipoyllysine-residue acetyltransferase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.3.1.12 2.3.1.12] </span></td></tr>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Electron Microscopy, [[Resolution|Resolution]] 3.84&#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=7q5r FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7q5r OCA], [https://pdbe.org/7q5r PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7q5r RCSB], [https://www.ebi.ac.uk/pdbsum/7q5r PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7q5r ProSAT]</span></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=7q5r FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7q5r OCA], [https://pdbe.org/7q5r PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7q5r RCSB], [https://www.ebi.ac.uk/pdbsum/7q5r PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7q5r ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
[[https://www.uniprot.org/uniprot/G0S4X6_CHATD G0S4X6_CHATD]] The pyruvate dehydrogenase complex catalyzes the overall conversion of pyruvate to acetyl-CoA and CO(2).[RuleBase:RU361137]
[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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== Publication Abstract from PubMed ==
== Publication Abstract from PubMed ==
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<div class="pdbe-citations 7q5r" style="background-color:#fffaf0;"></div>
<div class="pdbe-citations 7q5r" style="background-color:#fffaf0;"></div>
==See Also==
*[[Pyruvate dehydrogenase 3D structures|Pyruvate dehydrogenase 3D structures]]
== References ==
== References ==
<references/>
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Dihydrolipoyllysine-residue acetyltransferase]]
[[Category: Chaetomium thermophilum var. thermophilum DSM 1495]]
[[Category: Large Structures]]
[[Category: Large Structures]]
[[Category: Chojnowski, G]]
[[Category: Chojnowski G]]
[[Category: Hamdi, F]]
[[Category: Hamdi F]]
[[Category: Kastritis, P L]]
[[Category: Kastritis PL]]
[[Category: Kyrilis, F L]]
[[Category: Kyrilis FL]]
[[Category: Skalidis, I]]
[[Category: Skalidis I]]
[[Category: Tueting, C]]
[[Category: Tueting C]]
[[Category: Dihydrolipoyl]]
[[Category: E2]]
[[Category: Pyruvate]]
[[Category: Transacetylase]]
[[Category: Transferase]]

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