3beo

<table><tr><td colspan='2'>[[3beo]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/"bacillus_cereus_var._anthracis"_(cohn_1872)_smith_et_al._1946 "bacillus cereus var. anthracis" (cohn 1872) smith et al. 1946]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3BEO OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=3BEO FirstGlance]. <br>

</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=UD1:URIDINE-DIPHOSPHATE-N-ACETYLGLUCOSAMINE'>UD1</scene>, <scene name='pdbligand=UDP:URIDINE-5-DIPHOSPHATE'>UDP</scene></td></tr>

<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/UDP-N-acetylglucosamine_2-epimerase_(non-hydrolyzing) UDP-N-acetylglucosamine 2-epimerase (non-hydrolyzing)], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=5.1.3.14 5.1.3.14] </span></td></tr>

<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=3beo FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3beo OCA], [http://pdbe.org/3beo PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3beo RCSB], [http://www.ebi.ac.uk/pdbsum/3beo PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3beo ProSAT]</span></td></tr>

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== Publication Abstract from PubMed ==

The non-hydrolysing bacterial UDP-N-acetylglucosamine 2-epimerase (UDP-GlcNAc 2-epimerase) catalyses the conversion of UDP-GlcNAc into UDP-N-acetylmannosamine, an intermediate in the biosynthesis of several cell-surface polysaccharides. This enzyme is allosterically regulated by its substrate UDP-GlcNAc. The structure of the ternary complex between the Bacillus anthracis UDP-GlcNAc 2-epimerase, its substrate UDP-GlcNAc and the reaction intermediate UDP, showed direct interactions between UDP and its substrate, and between the complex and highly conserved enzyme residues, identifying the allosteric site of the enzyme. The binding of UDP-GlcNAc is associated with conformational changes in the active site of the enzyme. Kinetic data and mutagenesis of the highly conserved UDP-GlcNAc-interacting residues confirm their importance in the substrate binding and catalysis of the enzyme. This constitutes the first example to our knowledge, of an enzymatic allosteric activation by direct interaction between the substrate and the allosteric activator.

A structural basis for the allosteric regulation of non-hydrolysing UDP-GlcNAc 2-epimerases.,Velloso LM, Bhaskaran SS, Schuch R, Fischetti VA, Stebbins CE EMBO Rep. 2008 Feb;9(2):199-205. Epub 2008 Jan 11. PMID:18188181<ref>PMID:18188181</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 3beo" style="background-color:#fffaf0;"></div>

== References ==

<references/>

[[Category: Bhaskaran, S S]]

[[Category: Fischetti, V A]]

[[Category: Schuch, R]]

[[Category: Stebbins, C E]]

[[Category: Velloso, L M]]

[[Category: Udp-glcnac]]