View source for 5buv


==X-ray structure of WbcA from Yersinia enterocolitica==
<StructureSection load='5buv' size='340' side='right'caption='[[5buv]], [[Resolution|resolution]] 1.75&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[5buv]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Yersinia_enterocolitica_subsp._enterocolitica_8081 Yersinia enterocolitica subsp. enterocolitica 8081]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5BUV OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5BUV FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.75&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CYT:6-AMINOPYRIMIDIN-2(1H)-ONE'>CYT</scene>, <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene></td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=5buv FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5buv OCA], [https://pdbe.org/5buv PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5buv RCSB], [https://www.ebi.ac.uk/pdbsum/5buv PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5buv ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/A1JNA0_YERE8 A1JNA0_YERE8] 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Yersinia enterocolitica is a Gram-negative bacterium that causes yersiniosis, a zoonotic disease affecting the gastrointestinal tract of humans, cattle, and pigs, among others. The lipopolysaccharide of Y. enterocolitica O:8 contains an unusual sugar, 6-deoxy-d-gulose, which requires four enzymes for its biosynthesis. Here, we describe a combined structural and functional investigation of WbcA, which catalyzes the third step in the pathway, namely an epimerization about the C-3' carbon of a CDP-linked sugar. The structure of WbcA was determined to 1.75-A resolution, and the model was refined to an overall R-factor of 19.5%. The fold of WbcA places it into the well-defined cupin superfamily of sugar epimerases. Typically, these enzymes contain both a conserved histidine and a tyrosine residue that play key roles in catalysis. On the basis of amino acid sequence alignments, it was anticipated that the "conserved" tyrosine had been replaced with a cysteine residue in WbcA (Cys 133), and indeed this was the case. However, what was not anticipated was the fact that another tyrosine residue (Tyr 50) situated on a neighboring beta-strand moved into the active site. Site-directed mutant proteins were subsequently constructed and their kinetic properties analyzed to address the roles of Cys 133 and Tyr 50 in WbcA catalysis. This study emphasizes the continuing need to experimentally verify assumptions that are based solely on bioinformatics approaches. This article is protected by copyright. All rights reserved.

Biochemical studies on WbcA, a sugar epimerase from Yersinia enterocolitica.,Salinger AJ, Brown HA, Thoden JB, Holden HM Protein Sci. 2015 Jul 15. doi: 10.1002/pro.2747. PMID:26174084<ref>PMID:26174084</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 5buv" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Yersinia enterocolitica subsp. enterocolitica 8081]]
[[Category: Brown HA]]
[[Category: Holden HM]]
[[Category: Salinger AJ]]
[[Category: Thoden JB]]