Structural highlights
Function
[FCTA_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 PubMed
Crystal 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
- ↑ Gogos A, Gorman J, Shapiro L. Structure of Escherichia coli YfdW, a type III CoA transferase. Acta Crystallogr D Biol Crystallogr. 2004 Mar;60(Pt 3):507-11. Epub 2004, Feb 25. PMID:14993676 doi:10.1107/S0907444904000034
