7ott

<table><tr><td colspan='2'>[[7ott]] is a 1 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=7OTT OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7OTT 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>

== 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]

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== Publication Abstract from PubMed ==

Found across all kingdoms of life, 2-keto acid dehydrogenase complexes possess prominent metabolic roles and form major regulatory sites. Although their component structures are known, their higher-order organization is highly heterogeneous, not only across species or tissues but also even within a single cell. Here, we report a cryo-EM structure of the fully active Chaetomium thermophilum pyruvate dehydrogenase complex (PDHc) core scaffold at 3.85 A resolution (FSC = 0.143) from native cell extracts. By combining cryo-EM with macromolecular docking and molecular dynamics simulations, we resolve all PDHc core scaffold interfaces and dissect the residing transacetylase reaction. Electrostatics attract the lipoyl domain to the transacetylase active site and stabilize the coenzyme A, while apolar interactions position the lipoate in its binding cleft. Our results have direct implications on the structural determinants of the transacetylase reaction and the role of flexible regions in the context of the overall 10 MDa PDHc metabolon architecture.

Cryo-EM snapshots of a native lysate provide structural insights into a metabolon-embedded transacetylase reaction.,Tuting C, Kyrilis FL, Muller J, Sorokina M, Skalidis I, Hamdi F, Sadian Y, Kastritis PL Nat Commun. 2021 Nov 26;12(1):6933. doi: 10.1038/s41467-021-27287-4. PMID:34836937<ref>PMID:34836937</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>

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== References ==

<references/>

[[Category: Dihydrolipoyllysine-residue acetyltransferase]]

[[Category: Kastritis, P L]]

[[Category: Tueting, C]]

[[Category: Transferase]]