1vgr
From Proteopedia
| Line 1: | Line 1: | ||
[[Image:1vgr.jpg|left|200px]] | [[Image:1vgr.jpg|left|200px]] | ||
| - | + | <!-- | |
| - | + | The line below this paragraph, containing "STRUCTURE_1vgr", creates the "Structure Box" on the page. | |
| - | + | You may change the PDB parameter (which sets the PDB file loaded into the applet) | |
| - | + | or the SCENE parameter (which sets the initial scene displayed when the page is loaded), | |
| - | + | or leave the SCENE parameter empty for the default display. | |
| - | + | --> | |
| - | + | {{STRUCTURE_1vgr| PDB=1vgr | SCENE= }} | |
| - | + | ||
| - | + | ||
| - | }} | + | |
'''Formyl-CoA transferase mutant Asp169 to Glu''' | '''Formyl-CoA transferase mutant Asp169 to Glu''' | ||
| Line 30: | Line 27: | ||
[[Category: Ricagno, S.]] | [[Category: Ricagno, S.]] | ||
[[Category: Richards, N G.]] | [[Category: Richards, N G.]] | ||
| - | [[Category: | + | [[Category: Caib-baif family]] |
| - | [[Category: | + | [[Category: Coa complex]] |
| - | [[Category: | + | [[Category: Coa transferase]] |
| - | [[Category: | + | [[Category: Intertwined]] |
| - | [[Category: | + | [[Category: Knotted fold]] |
| - | [[Category: | + | [[Category: Oxalate]] |
| - | [[Category: | + | [[Category: Oxalate degradation]] |
| - | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 12:31:26 2008'' | |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | |
Revision as of 09:31, 3 May 2008
Formyl-CoA transferase mutant Asp169 to Glu
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
1VGR is a Single protein structure of sequence from Oxalobacter formigenes. 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 Page seeded by OCA on Sat May 3 12:31:26 2008
