7bgj: Difference between revisions

← Older edit

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

OCA

@@ Line 1: / Line 1: @@
-'''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]]