2gz6: Difference between revisions

Revision as of 23:47, 28 July 2008

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File:2gz6.png

Template:STRUCTURE 2gz6

Crystal Structure Of Anabaena sp. CH1 N-acetyl-D-glucosamine 2-epimerase At 2.0 ACrystal Structure Of Anabaena sp. CH1 N-acetyl-D-glucosamine 2-epimerase At 2.0 A

Template:ABSTRACT PUBMED 17292397

About this StructureAbout this Structure

Full crystallographic information is available from OCA.

ReferenceReference

The central cavity from the (alpha/alpha)6 barrel structure of Anabaena sp. CH1 N-acetyl-D-glucosamine 2-epimerase contains two key histidine residues for reversible conversion., Lee YC, Wu HM, Chang YN, Wang WC, Hsu WH, J Mol Biol. 2007 Mar 30;367(3):895-908. Epub 2006 Nov 6. PMID:17292397

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-'''Crystal Structure Of Anabaena sp. CH1 N-acetyl-D-glucosamine 2-epimerase At 2.0 A'''
+===Crystal Structure Of Anabaena sp. CH1 N-acetyl-D-glucosamine 2-epimerase At 2.0 A===
-==Overview==
+<!--
-N-acetyl-D-glucosamine 2-epimerase (GlcNAc 2-epimerase) catalyzes the reversible epimerization between N-acetyl-D-glucosamine (GlcNAc) and N-acetyl-D-mannosamine (ManNAc). We report here the 2.0 A resolution crystal structure of the GlcNAc 2-epimerase from Anabaena sp. CH1. The structure demonstrates an (alpha/alpha)(6) barrel fold, which shows structural homology with porcine GlcNAc 2-epimerase as well as a number of glycoside hydrolase enzymes and other sugar-metabolizing enzymes. One side of the barrel structure consists of short loops involved in dimer interactions. The other side of the barrel structure is comprised of long loops containing six short beta-sheets, which enclose a putative central active-site pocket. Site-directed mutagenesis of conserved residues near the N-terminal region of the inner alpha helices shows that R57, H239, E308, and H372 are strictly required for activity. E242 and R375 are also essential in catalysis. Based on the structure and kinetic analysis, H239 and H372 may serve as the key active site acid/base catalysts. These results suggest that the (alpha/alpha)(6) barrel represents a steady fold for presenting active-site residues in a cleft at the N-terminal ends of the inner alpha helices, thus forming a fine-tuned catalytic site in GlcNAc 2-epimerase.
+The line below this paragraph, {{ABSTRACT_PUBMED_17292397}}, adds the Publication Abstract to the page
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+{{ABSTRACT_PUBMED_17292397}}
 ==About this Structure==
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 [[Category: Anabaena sp. ch1]]
 [[Category: N-acetyl-d-glucosamine 2-epimerase]]
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