3beo
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(New page: 200px<br /><applet load="3beo" size="350" color="white" frame="true" align="right" spinBox="true" caption="3beo, resolution 1.700Å" /> '''A Structural Basis ...)
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Revision as of 17:05, 21 February 2008
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A Structural Basis for the allosteric regulation of non-hydrolyzing UDP-GlcNAc 2-epimerases
Overview
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.
About this Structure
3BEO is a Single protein structure of sequence from Bacillus anthracis with and as ligands. Active as UDP-N-acetylglucosamine 2-epimerase, with EC number 5.1.3.14 Known structural/functional Sites: , , and . Full crystallographic information is available from OCA.
Reference
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
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