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TitleStructural analysis of an endogenous 4-megadalton succinyl-CoA-generating metabolon.
Journal, issue, pagesCommun Biol, Vol. 6, Issue 1, Page 552, Year 2023
Publish dateMay 22, 2023
AuthorsIoannis Skalidis / Fotis L Kyrilis / Christian Tüting / Farzad Hamdi / Toni K Träger / Jaydeep Belapure / Gerd Hause / Marta Fratini / Francis J O'Reilly / Ingo Heilmann / Juri Rappsilber / Panagiotis L Kastritis /
PubMed AbstractThe oxoglutarate dehydrogenase complex (OGDHc) participates in the tricarboxylic acid cycle and, in a multi-step reaction, decarboxylates α-ketoglutarate, transfers succinyl to CoA, and reduces NAD+. ...The oxoglutarate dehydrogenase complex (OGDHc) participates in the tricarboxylic acid cycle and, in a multi-step reaction, decarboxylates α-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 Å 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.
External linksCommun Biol / PubMed:37217784 / PubMed Central
MethodsEM (single particle)
Resolution3.35 Å
Structure data

16900

8oiu

EMDB-16900, PDB-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
Method: EM (single particle) / Resolution: 3.35 Å

Source
  • thermochaetoides thermophila dsm 1495 (fungus)
KeywordsTRANSFERASE / Dihydrolipoyl Succinyltransferase / E2 / Oxoglutarate / a-Ketoglutarate

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