1VGR

Formyl-CoA transferase mutant Asp169 to Glu

Summary for 1VGR

• Entry DOI: 10.2210/pdb1vgr/pdb
• Related: 1p5h 1p5r 1t3z 1vgq
• Descriptor: Formyl-coenzyme A transferase, COENZYME A (3 entities in total)
• Functional Keywords: coa transferase, oxalate, oxalate degradation, intertwined, knotted fold, caib-baif family, coa complex, transferase
• Biological source: Oxalobacter formigenes
• Cellular location: Cytoplasm: O06644
• Total number of polymer chains: 2
• Total formula weight: 96026.45

Authors

Ricagno, S.,Jonsson, S.,Richards, N.G.,Lindqvist, Y. (deposition date: 2004-04-28, release date: 2004-08-03, Last modification date: 2023-10-25)

Primary citation

Jonsson, S.,Ricagno, S.,Lindqvist, Y.,Richards, N.G.
Kinetic and mechanistic characterization of the formyl-CoA transferase from Oxalobacter formigenes
J.Biol.Chem., 279:36003-36012, 2004

PubMed Abstract: Oxalobacter formigenes is an obligate anaerobe that colonizes the human gastrointestinal tract and employs oxalate breakdown to generate ATP in a novel process involving the interplay of two coupled enzymes and a membrane-bound oxalate:formate antiporter. Formyl-CoA transferase is a critical enzyme in oxalate-dependent ATP synthesis and is the first Class III CoA-transferase for which a high resolution, three-dimensional structure has been determined (Ricagno, S., Jonsson, S., Richards, N., and Lindqvist, Y. (2003) EMBO J. 22, 3210-3219). We now report the first detailed kinetic characterizations of recombinant, wild type formyl-CoA transferase and a number of site-specific mutants, which suggest that catalysis proceeds via a series of anhydride intermediates. Further evidence for this mechanistic proposal is provided by the x-ray crystallographic observation of an acylenzyme intermediate that is formed when formyl-CoA transferase is incubated with oxalyl-CoA. The catalytic mechanism of formyl-CoA transferase is therefore established and is almost certainly employed by all other members of the Class III CoA-transferase family.

PubMed: 15213226
DOI: 10.1074/jbc.M404873200

Experimental method

X-RAY DIFFRACTION (2.1 Å)