Single particle cryo-EM structure of the homohexameric 2-oxoglutarate dehydrogenase OdhA from Corynebacterium glutamicumSingle particle cryo-EM structure of the homohexameric 2-oxoglutarate dehydrogenase OdhA from Corynebacterium glutamicum

Structural highlights

8p5t is a 6 chain structure with sequence from Corynebacterium glutamicum ATCC 13032. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:Electron Microscopy, Resolution 2.17Å
Ligands:, ,
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

ODO12_CORGL Catalyzes the E1 and E2 reactions as part of 2-oxoglutarate dehydrogenase (ODH) activity, to convert 2-oxoglutarate to succinyl-CoA and CO(2). OdhA has reductase activity with 2-oxoglutarate but does not react with pyruvate, and also displays transsuccinylase but no transacetylase activity. Since OdhA is not lipoylated, the succinyltransferase activity of its E2 domain is dependent on lipoyl residues of the acetyltransferase AceF.[1]

References

  1. Hoffelder M, Raasch K, van Ooyen J, Eggeling L. The E2 domain of OdhA of Corynebacterium glutamicum has succinyltransferase activity dependent on lipoyl residues of the acetyltransferase AceF. J Bacteriol. 2010 Oct;192(19):5203-11. doi: 10.1128/JB.00597-10. Epub 2010 Jul, 30. PMID:20675489 doi:http://dx.doi.org/10.1128/JB.00597-10

8p5t, resolution 2.17Å

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