2q27

<StructureSection load='2q27' size='340' side='right' caption='[[2q27]], [[Resolution|resolution]] 2.12&Aring;' scene=''>

<table><tr><td colspan='2'>[[2q27]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2Q27 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2Q27 FirstGlance]. <br>

</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=MES:2-(N-MORPHOLINO)-ETHANESULFONIC+ACID'>MES</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>, <scene name='pdbligand=TPP:THIAMINE+DIPHOSPHATE'>TPP</scene></td></tr>

<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Oxalyl-CoA_decarboxylase Oxalyl-CoA decarboxylase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=4.1.1.8 4.1.1.8] </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=2q27 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2q27 OCA], [http://pdbe.org/2q27 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2q27 RCSB], [http://www.ebi.ac.uk/pdbsum/2q27 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2q27 ProSAT]</span></td></tr>

<scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/q2/2q27_consurf.spt"</scriptWhenChecked>

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== Publication Abstract from PubMed ==

The gene yfdU from Escherichia coli encodes a putative oxalyl coenzyme A decarboxylase, a thiamine diphosphate-dependent enzyme that is potentially involved in the degradation of oxalate. The enzyme has been purified to homogeneity. The kinetic constants for conversion of the substrate oxalyl coenzyme A by the enzyme in the absence and presence of the inhibitor coenzyme A, as well as in the absence and presence of the activator adenosine 5'-diphosphate, were determined using a novel continuous optical assay. The effects of these ligands on the solution and crystal structure of the enzyme were studied using small-angle X-ray scattering and X-ray crystal diffraction. Analyses of the obtained crystal structures of the enzyme in complex with the cofactor thiamine diphosphate, the activator adenosine 5'-diphosphate and the inhibitor acetyl coenzyme A, as well as the corresponding solution scattering patterns, allow comparison of the oligomer structures of the enzyme complexes under various experimental conditions, and provide insights into the architecture of substrate and effector binding sites.

New insights into structure-function relationships of oxalyl CoA decarboxylase from Escherichia coli.,Werther T, Zimmer A, Wille G, Golbik R, Weiss MS, Konig S FEBS J. 2010 Jun;277(12):2628-40. PMID:20553497<ref>PMID:20553497</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>

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<div class="pdbe-citations 2q27" style="background-color:#fffaf0;"></div>

== References ==

<references/>

[[Category: Escherichia coli]]

[[Category: Oxalyl-CoA decarboxylase]]

[[Category: Hubner, G]]

[[Category: Konig, S]]

[[Category: Weiss, M S]]

[[Category: Werther, T]]

[[Category: Wille, G]]

[[Category: Zimmer, A]]

[[Category: Thiamine diphosphate]]