4kgb
From Proteopedia
Structure of succinyl-CoA: 3-ketoacid CoA transferase from Drosophila melanogaster
Structural highlights
FunctionSCOT_DROME Key enzyme for ketone body catabolism (PubMed:24100554). Transfers the CoA moiety from succinate to acetoacetate (PubMed:24100554). Formation of the enzyme-CoA intermediate proceeds via an unstable anhydride species formed between the carboxylate groups of the enzyme and substrate (By similarity).[UniProtKB:Q29551][1] Publication Abstract from PubMedSuccinyl-CoA:3-ketoacid CoA transferase (SCOT) plays a crucial role in ketone-body metabolism. SCOT from Drosophila melanogaster (DmSCOT) was purified and crystallized. The crystal structure of DmSCOT was determined at 2.64 A resolution and belonged to space group P212121, with unit-cell parameters a = 76.638, b = 101.921, c = 122.457 A, alpha = beta = gamma = 90 degrees . Sequence alignment and structural analysis identified DmSCOT as a class I CoA transferase. Compared with Acetobacter aceti succinyl-CoA:acetate CoA transferase, DmSCOT has a different substrate-binding pocket, which may explain the difference in their substrate specificities. Structure of succinyl-CoA:3-ketoacid CoA transferase from Drosophila melanogaster.,Zhang M, Xu HY, Wang YC, Shi ZB, Zhang NN Acta Crystallogr Sect F Struct Biol Cryst Commun. 2013 Oct;69(Pt 10):1089-93., doi: 10.1107/S1744309113024986. Epub 2013 Sep 28. PMID:24100554[2] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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