1vgq: Difference between revisions
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'''Formyl-CoA transferase mutant Asp169 to Ala''' | {{Structure | ||
|PDB= 1vgq |SIZE=350|CAPTION= <scene name='initialview01'>1vgq</scene>, resolution 2.13Å | |||
|SITE= | |||
|LIGAND= <scene name='pdbligand=CAO:OXIDIZED COENZYME A'>CAO</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 Ala''' | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
1VGQ is a [ | 1VGQ 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=1VGQ 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 14:45:20 2008'' | ||
Revision as of 12:45, 20 March 2008
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| 1vgq, resolution 2.13Å | |||||||||||||
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| Ligands: | CAO | ||||||||||||
| 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 Ala
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
1VGQ 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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