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1vgr

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[[Image:1vgr.jpg|left|200px]]
 
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{{Structure
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==Formyl-CoA transferase mutant Asp169 to Glu==
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|PDB= 1vgr |SIZE=350|CAPTION= <scene name='initialview01'>1vgr</scene>, resolution 2.10&Aring;
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<StructureSection load='1vgr' size='340' side='right'caption='[[1vgr]], [[Resolution|resolution]] 2.10&Aring;' scene=''>
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|SITE=
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== Structural highlights ==
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|LIGAND= <scene name='pdbligand=COA:COENZYME A'>COA</scene>
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<table><tr><td colspan='2'>[[1vgr]] is a 2 chain structure with sequence from [https://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]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1VGR FirstGlance]. <br>
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|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]
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.1&#8491;</td></tr>
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|GENE= FRC ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=847 Oxalobacter formigenes])
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=COA:COENZYME+A'>COA</scene></td></tr>
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}}
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1vgr FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1vgr OCA], [https://pdbe.org/1vgr PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1vgr RCSB], [https://www.ebi.ac.uk/pdbsum/1vgr PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1vgr ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/FCTA_OXAFO FCTA_OXAFO] Catalyzes the transfer of the CoA moiety from formyl-CoA to oxalate. Essential enzyme for the bacterium survival, as it relies on oxalic acid as its sole source of energy.[HAMAP-Rule:MF_00742]
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/vg/1vgr_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1vgr ConSurf].
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<div style="clear:both"></div>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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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.
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'''Formyl-CoA transferase mutant Asp169 to Glu'''
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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<ref>PMID:15213226</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 1vgr" style="background-color:#fffaf0;"></div>
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==Overview==
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==See Also==
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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.
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*[[Formyl-CoA transferase|Formyl-CoA transferase]]
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== References ==
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==About this Structure==
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<references/>
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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].
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__TOC__
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</StructureSection>
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==Reference==
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[[Category: Large Structures]]
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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]
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[[Category: Formyl-CoA transferase]]
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[[Category: Oxalobacter formigenes]]
[[Category: Oxalobacter formigenes]]
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[[Category: Single protein]]
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[[Category: Jonsson S]]
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[[Category: Jonsson, S.]]
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[[Category: Lindqvist Y]]
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[[Category: Lindqvist, Y.]]
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[[Category: Ricagno S]]
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[[Category: Ricagno, S.]]
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[[Category: Richards NG]]
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[[Category: Richards, N G.]]
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[[Category: COA]]
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[[Category: caib-baif family]]
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[[Category: coa complex]]
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[[Category: coa transferase]]
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[[Category: intertwined]]
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[[Category: knotted fold]]
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[[Category: oxalate]]
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[[Category: oxalate degradation]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 14:45:22 2008''
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Current revision

Formyl-CoA transferase mutant Asp169 to Glu

PDB ID 1vgr

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