View source for 8oiu


==Cryo-EM reconstruction of the native 24-mer E2o core of the 2-oxoglutarate dehydrogenase complex of C. thermophilum at 3.35 A resolution==
<StructureSection load='8oiu' size='340' side='right'caption='[[8oiu]], [[Resolution|resolution]] 3.35&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[8oiu]] 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=8OIU OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=8OIU 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]] 3.35&#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=8oiu FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8oiu OCA], [https://pdbe.org/8oiu PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8oiu RCSB], [https://www.ebi.ac.uk/pdbsum/8oiu PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8oiu ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/G0SAX9_CHATD G0SAX9_CHATD] 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
The oxoglutarate dehydrogenase complex (OGDHc) participates in the tricarboxylic acid cycle and, in a multi-step reaction, decarboxylates alpha-ketoglutarate, transfers succinyl to CoA, and reduces NAD+. Due to its pivotal role in metabolism, OGDHc enzymatic components have been studied in isolation; however, their interactions within the endogenous OGDHc remain elusive. Here, we discern the organization of a thermophilic, eukaryotic, native OGDHc in its active state. By combining biochemical, biophysical, and bioinformatic methods, we resolve its composition, 3D architecture, and molecular function at 3.35 A resolution. We further report the high-resolution cryo-EM structure of the OGDHc core (E2o), which displays various structural adaptations. These include hydrogen bonding patterns confining interactions of OGDHc participating enzymes (E1o-E2o-E3), electrostatic tunneling that drives inter-subunit communication, and the presence of a flexible subunit (E3BPo), connecting E2o and E3. This multi-scale analysis of a succinyl-CoA-producing native cell extract provides a blueprint for structure-function studies of complex mixtures of medical and biotechnological value.

Structural analysis of an endogenous 4-megadalton succinyl-CoA-generating metabolon.,Skalidis I, Kyrilis FL, Tuting C, Hamdi F, Trager TK, Belapure J, Hause G, Fratini M, O'Reilly FJ, Heilmann I, Rappsilber J, Kastritis PL Commun Biol. 2023 May 22;6(1):552. doi: 10.1038/s42003-023-04885-0. PMID:37217784<ref>PMID:37217784</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 8oiu" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Chaetomium thermophilum var. thermophilum DSM 1495]]
[[Category: Large Structures]]
[[Category: Hamdi F]]
[[Category: Kastritis PL]]
[[Category: Kyrilis FL]]
[[Category: Skalidis I]]
[[Category: Tueting C]]