1vgr
From Proteopedia
(New page: 200px<br /><applet load="1vgr" size="450" color="white" frame="true" align="right" spinBox="true" caption="1vgr, resolution 2.10Å" /> '''Formyl-CoA transfera...) |
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| - | [[Image:1vgr.jpg|left|200px]]<br /><applet load="1vgr" size=" | + | [[Image:1vgr.jpg|left|200px]]<br /><applet load="1vgr" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1vgr, resolution 2.10Å" /> | caption="1vgr, resolution 2.10Å" /> | ||
'''Formyl-CoA transferase mutant Asp169 to Glu'''<br /> | '''Formyl-CoA transferase mutant Asp169 to Glu'''<br /> | ||
==Overview== | ==Overview== | ||
| - | Oxalobacter formigenes is an obligate anaerobe that colonizes the human | + | 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== | ==About this Structure== | ||
| - | 1VGR is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Oxalobacter_formigenes Oxalobacter formigenes] with COA as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [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] Full crystallographic information is available from [http:// | + | 1VGR is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Oxalobacter_formigenes Oxalobacter formigenes] with <scene name='pdbligand=COA:'>COA</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [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] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1VGR OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Lindqvist, Y.]] | [[Category: Lindqvist, Y.]] | ||
[[Category: Ricagno, S.]] | [[Category: Ricagno, S.]] | ||
| - | [[Category: Richards, N | + | [[Category: Richards, N G.]] |
[[Category: COA]] | [[Category: COA]] | ||
[[Category: caib-baif family]] | [[Category: caib-baif family]] | ||
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[[Category: oxalate degradation]] | [[Category: oxalate degradation]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 15:35:07 2008'' |
Revision as of 13:35, 21 February 2008
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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 with 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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