1t4c
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(New page: 200px<br /><applet load="1t4c" size="450" color="white" frame="true" align="right" spinBox="true" caption="1t4c, resolution 2.61Å" /> '''Formyl-CoA Transfera...)
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Revision as of 00:51, 21 November 2007
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Formyl-CoA Transferase in complex with Oxalyl-CoA
Overview
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.
About this Structure
1T4C is a Protein complex structure of sequences from Oxalobacter formigenes with COA as ligand. Active as Formyl-CoA transferase, with EC number 2.8.3.16 Full crystallographic information is available from OCA.
Reference
Kinetic and mechanistic characterization of the formyl-CoA transferase from Oxalobacter formigenes., Jonsson S, Ricagno S, Lindqvist Y, Richards NG, J Biol Chem. 2004 Aug 20;279(34):36003-12. Epub 2004 Jun 21. PMID:15213226
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