View source for 2vjp

==FORMYL-COA TRANSFERASE MUTANT VARIANT W48F==
<StructureSection load='2vjp' size='340' side='right' caption='[[2vjp]], [[Resolution|resolution]] 1.95&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[2vjp]] is a 2 chain structure with 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=2VJP OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2VJP FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=NA:SODIUM+ION'>NA</scene></td></tr>
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2vjo|2vjo]], [[1vgq|1vgq]], [[1vgr|1vgr]], [[1p5h|1p5h]], [[1t4c|1t4c]], [[2vjl|2vjl]], [[1t3z|1t3z]], [[2vjn|2vjn]], [[1p5r|1p5r]], [[2vjq|2vjq]], [[2vjk|2vjk]], [[2vjm|2vjm]]</td></tr>
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><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></td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2vjp FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2vjp OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2vjp RCSB], [http://www.ebi.ac.uk/pdbsum/2vjp PDBsum]</span></td></tr>
</table>
== Function ==
[[http://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] 
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
Check<jmol>
  <jmolCheckbox>
    <scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/vj/2vjp_consurf.spt"</scriptWhenChecked>
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
    <text>to colour the structure by Evolutionary Conservation</text>
  </jmolCheckbox>
</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/chain_selection.php?pdb_ID=2ata ConSurf].
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
The yfdXWUVE operon appears to encode proteins that enhance the ability of Escherichia coli MG1655 to survive under acidic conditions. Although the molecular mechanisms underlying this phenotypic behavior remain to be elucidated, findings from structural genomic studies have shown that the structure of YfdW, the protein encoded by the yfdW gene, is homologous to that of the enzyme that mediates oxalate catabolism in the obligate anaerobe Oxalobacter formigenes, O. formigenes formyl coenzyme A transferase (FRC). We now report the first detailed examination of the steady-state kinetic behavior and substrate specificity of recombinant, wild-type YfdW. Our studies confirm that YfdW is a formyl coenzyme A (formyl-CoA) transferase, and YfdW appears to be more stringent than the corresponding enzyme (FRC) in Oxalobacter in employing formyl-CoA and oxalate as substrates. We also report the effects of replacing Trp-48 in the FRC active site with the glutamine residue that occupies an equivalent position in the E. coli protein. The results of these experiments show that Trp-48 precludes oxalate binding to a site that mediates substrate inhibition for YfdW. In addition, the replacement of Trp-48 by Gln-48 yields an FRC variant for which oxalate-dependent substrate inhibition is modified to resemble that seen for YfdW. Our findings illustrate the utility of structural homology in assigning enzyme function and raise the question of whether oxalate catabolism takes place in E. coli upon the up-regulation of the yfdXWUVE operon under acidic conditions.

Differential substrate specificity and kinetic behavior of Escherichia coli YfdW and Oxalobacter formigenes formyl coenzyme A transferase.,Toyota CG, Berthold CL, Gruez A, Jonsson S, Lindqvist Y, Cambillau C, Richards NG J Bacteriol. 2008 Apr;190(7):2556-64. Epub 2008 Feb 1. PMID:18245280<ref>PMID:18245280</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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==See Also==
*[[Formyl-CoA transferase|Formyl-CoA transferase]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Formyl-CoA transferase]]
[[Category: Oxalobacter formigenes]]
[[Category: Berthold, C L]]
[[Category: Cambillau, C]]
[[Category: Gruez, A]]
[[Category: Jonsson, S]]
[[Category: Lindqvist, Y]]
[[Category: Richards, N G.J]]
[[Category: Toyota, C G]]
[[Category: Class iii coa transferase]]
[[Category: Transferase]]