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1T4C

Formyl-CoA Transferase in complex with Oxalyl-CoA

Summary for 1T4C
Entry DOI10.2210/pdb1t4c/pdb
Related1p5h 1p5r 1t3z 1vgq 1vgr
DescriptorFormyl-CoA:oxalate CoA-transferase, COENZYME A, OXALIC ACID, ... (4 entities in total)
Functional Keywordscoa transferase, oxalate, oxalate degradation, intertwined, knotted fold, caib-baif family, oxalyl-coa, anhydride, transferase
Biological sourceOxalobacter formigenes
Total number of polymer chains2
Total formula weight96088.44
Authors
Ricagno, S.,Jonsson, S.,Richards, N.G.,Lindqvist, Y. (deposition date: 2004-04-29, release date: 2004-08-03, Last modification date: 2024-10-09)
Primary citationJonsson, 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
Cited by
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
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (2.61 Å)
Structure validation

237735

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