1vgr
From Proteopedia
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| - | [[Image:1vgr.jpg|left|200px]] | + | [[Image:1vgr.jpg|left|200px]] |
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| - | '''Formyl-CoA transferase mutant Asp169 to Glu''' | + | {{Structure |
| + | |PDB= 1vgr |SIZE=350|CAPTION= <scene name='initialview01'>1vgr</scene>, resolution 2.10Å | ||
| + | |SITE= | ||
| + | |LIGAND= <scene name='pdbligand=COA:COENZYME A'>COA</scene> | ||
| + | |ACTIVITY= [http://en.wikipedia.org/wiki/Formyl-CoA_transferase Formyl-CoA transferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.8.3.16 2.8.3.16] | ||
| + | |GENE= FRC ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=847 Oxalobacter formigenes]) | ||
| + | }} | ||
| + | |||
| + | '''Formyl-CoA transferase mutant Asp169 to Glu''' | ||
| + | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1VGR is a [ | + | 1VGR is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Oxalobacter_formigenes Oxalobacter formigenes]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1VGR OCA]. |
==Reference== | ==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:[http:// | + | 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:[http://www.ncbi.nlm.nih.gov/pubmed/15213226 15213226] |
[[Category: Formyl-CoA transferase]] | [[Category: Formyl-CoA transferase]] | ||
[[Category: Oxalobacter formigenes]] | [[Category: Oxalobacter formigenes]] | ||
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[[Category: oxalate degradation]] | [[Category: oxalate degradation]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 14:45:22 2008'' |
Revision as of 12:45, 20 March 2008
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| , resolution 2.10Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | |||||||
| Gene: | FRC (Oxalobacter formigenes) | ||||||
| Activity: | Formyl-CoA transferase, with EC number 2.8.3.16 | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
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
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