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| <StructureSection load='7b9k' size='340' side='right'caption='[[7b9k]], [[Resolution|resolution]] 3.16Å' scene=''> | | <StructureSection load='7b9k' size='340' side='right'caption='[[7b9k]], [[Resolution|resolution]] 3.16Å' scene=''> |
| == Structural highlights == | | == Structural highlights == |
| <table><tr><td colspan='2'>[[7b9k]] is a 24 chain structure with sequence from [https://en.wikipedia.org/wiki/Ecoli Ecoli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7B9K OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7B9K FirstGlance]. <br> | | <table><tr><td colspan='2'>Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7B9K OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7B9K FirstGlance]. <br> |
| </td></tr><tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=LA2:N~6~-[(6R)-6,8-DISULFANYLOCTANOYL]-L-LYSINE'>LA2</scene></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]] 3.16Å</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> | | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=LA2:N~6~-[(6R)-6,8-DISULFANYLOCTANOYL]-L-LYSINE'>LA2</scene></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=7b9k FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7b9k OCA], [https://pdbe.org/7b9k PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7b9k RCSB], [https://www.ebi.ac.uk/pdbsum/7b9k PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7b9k 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=7b9k FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7b9k OCA], [https://pdbe.org/7b9k PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7b9k RCSB], [https://www.ebi.ac.uk/pdbsum/7b9k PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7b9k ProSAT]</span></td></tr> |
| </table> | | </table> |
| == Function ==
| |
| [[https://www.uniprot.org/uniprot/ODP2_ECOLI ODP2_ECOLI]] The pyruvate dehydrogenase complex catalyzes the overall conversion of pyruvate to acetyl-CoA and CO(2). It contains multiple copies of three enzymatic components: pyruvate dehydrogenase (E1), dihydrolipoamide acetyltransferase (E2) and lipoamide dehydrogenase (E3).
| |
| <div style="background-color:#fffaf0;">
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| == Publication Abstract from PubMed ==
| |
| The pyruvate dehydrogenase complex (PDHc) links glycolysis to the citric acid cycle by converting pyruvate into acetyl-coenzyme A. PDHc encompasses three enzymatically active subunits, namely pyruvate dehydrogenase, dihydrolipoyl transacetylase, and dihydrolipoyl dehydrogenase. Dihydrolipoyl transacetylase is a multidomain protein comprising a varying number of lipoyl domains, a peripheral subunit-binding domain, and a catalytic domain. It forms the structural core of the complex, provides binding sites for the other enzymes, and shuffles reaction intermediates between the active sites through covalently bound lipoyl domains. The molecular mechanism by which this shuttling occurs has remained elusive. Here, we report a cryo-EM reconstruction of the native E. coli dihydrolipoyl transacetylase core in a resting state. This structure provides molecular details of the assembly of the core and reveals how the lipoyl domains interact with the core at the active site.
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| Structure of the native pyruvate dehydrogenase complex reveals the mechanism of substrate insertion.,Skerlova J, Berndtsson J, Nolte H, Ott M, Stenmark P Nat Commun. 2021 Sep 6;12(1):5277. doi: 10.1038/s41467-021-25570-y. PMID:34489474<ref>PMID:34489474</ref>
| | ==See Also== |
| | | *[[Dihydrolipoamide acetyltransferase 3D structures|Dihydrolipoamide acetyltransferase 3D structures]] |
| From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
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| </div>
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| <div class="pdbe-citations 7b9k" style="background-color:#fffaf0;"></div>
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| == References == | |
| <references/>
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| __TOC__ | | __TOC__ |
| </StructureSection> | | </StructureSection> |
| [[Category: Dihydrolipoyllysine-residue acetyltransferase]]
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| [[Category: Ecoli]]
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| [[Category: Large Structures]] | | [[Category: Large Structures]] |
| [[Category: Skerlova, J]] | | [[Category: Skerlova J]] |
| [[Category: Stenmark, P]] | | [[Category: Stenmark P]] |
| [[Category: Dihydrolipoyllysine]]
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| [[Category: Lipoic acid]]
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| [[Category: Multienzyme complex]]
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| [[Category: Oxoacid dehydrogenase complex]]
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| [[Category: Transferase]]
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