1vgq: Difference between revisions
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|PDB= 1vgq |SIZE=350|CAPTION= <scene name='initialview01'>1vgq</scene>, resolution 2.13Å | |PDB= 1vgq |SIZE=350|CAPTION= <scene name='initialview01'>1vgq</scene>, resolution 2.13Å | ||
|SITE= | |SITE= | ||
|LIGAND= <scene name='pdbligand=CAO:OXIDIZED COENZYME A'>CAO</scene> | |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] | |ACTIVITY= <span class='plainlinks'>[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] </span> | ||
|GENE= FRC ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=847 Oxalobacter formigenes]) | |GENE= FRC ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=847 Oxalobacter formigenes]) | ||
|DOMAIN= | |||
|RELATEDENTRY=[[1p5h|1p5h]], [[1p5r|1p5r]], [[1vgr|1vgr]], [[1t3z|1t3z]] | |||
|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1vgq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1vgq OCA], [http://www.ebi.ac.uk/pdbsum/1vgq PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1vgq RCSB]</span> | |||
}} | }} | ||
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[[Category: Ricagno, S.]] | [[Category: Ricagno, S.]] | ||
[[Category: Richards, N G.]] | [[Category: Richards, N G.]] | ||
[[Category: caib-baif family]] | [[Category: caib-baif family]] | ||
[[Category: coa complex]] | [[Category: coa complex]] | ||
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[[Category: oxalate degradation]] | [[Category: oxalate degradation]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 00:24:19 2008'' | ||
Revision as of 21:24, 30 March 2008
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| 1vgq, resolution 2.13Å | |||||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
| Ligands: | CAO | ||||||||||||
| Gene: | FRC (Oxalobacter formigenes) | ||||||||||||
| Activity: | Formyl-CoA transferase, with EC number 2.8.3.16 | ||||||||||||
| Related: | 1p5h, 1p5r, 1vgr, 1t3z
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| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||||||||
| 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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