1q7e
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Crystal Structure of YfdW protein from E. coli
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Structural highlights
FunctionFCTA_ECOLI Catalyzes the transfer of the CoA moiety from formyl-CoA to oxalate. Evolutionary Conservation![]() Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedCrystal structures are reported for free and coenzyme A (CoA) bound forms of the YfdW protein from Escherichia coli, a representative type III CoA transferase. The structures reveal a two-domain protomer with interdomain connections forming a ring-like structure with a large central hole. Two protomers associate to form a highly intertwined dimer in which the hole of each ring is filled by the partner molecule. Each protomer binds a single CoA molecule and these CoA-binding sites are distant from one another in the dimer. Structure of Escherichia coli YfdW, a type III CoA transferase.,Gogos A, Gorman J, Shapiro L Acta Crystallogr D Biol Crystallogr. 2004 Mar;60(Pt 3):507-11. Epub 2004, Feb 25. PMID:14993676[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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