2chn: Difference between revisions

Revision as of 08:09, 28 July 2008

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File:2chn.png

Template:STRUCTURE 2chn

BACTEROIDES THETAIOTAOMICRON HEXOSAMINIDASE WITH O-GLCNACASE ACTIVITY- NAG-THIAZOLINE COMPLEXBACTEROIDES THETAIOTAOMICRON HEXOSAMINIDASE WITH O-GLCNACASE ACTIVITY- NAG-THIAZOLINE COMPLEX

Template:ABSTRACT PUBMED 16565725

About this StructureAbout this Structure

2CHN is a Protein complex structure of sequences from Bacteroides thetaiotaomicron. Full crystallographic information is available from OCA.

ReferenceReference

Structure and mechanism of a bacterial beta-glucosaminidase having O-GlcNAcase activity., Dennis RJ, Taylor EJ, Macauley MS, Stubbs KA, Turkenburg JP, Hart SJ, Black GN, Vocadlo DJ, Davies GJ, Nat Struct Mol Biol. 2006 Apr;13(4):365-71. Epub 2006 Mar 26. PMID:16565725

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Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA

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 {{STRUCTURE_2chn|  PDB=2chn  |  SCENE=  }}
-'''BACTEROIDES THETAIOTAOMICRON HEXOSAMINIDASE WITH O-GLCNACASE ACTIVITY- NAG-THIAZOLINE COMPLEX'''
+===BACTEROIDES THETAIOTAOMICRON HEXOSAMINIDASE WITH O-GLCNACASE ACTIVITY- NAG-THIAZOLINE COMPLEX===
-==Overview==
+<!--
-O-GlcNAc is an abundant post-translational modification of serine and threonine residues of nucleocytoplasmic proteins. This modification, found only within higher eukaryotes, is a dynamic modification that is often reciprocal to phosphorylation. In a manner analogous to phosphatases, a glycoside hydrolase termed O-GlcNAcase cleaves O-GlcNAc from modified proteins. Enzymes with high sequence similarity to human O-GlcNAcase are also found in human pathogens and symbionts. We report the three-dimensional structure of O-GlcNAcase from the human gut symbiont Bacteroides thetaiotaomicron both in its native form and in complex with a mimic of the reaction intermediate. Mutagenesis and kinetics studies show that the bacterial enzyme, very similarly to its human counterpart, operates via an unusual 'substrate-assisted' catalytic mechanism, which will inform the rational design of enzyme inhibitors.
+The line below this paragraph, {{ABSTRACT_PUBMED_16565725}}, adds the Publication Abstract to the page
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+{{ABSTRACT_PUBMED_16565725}}
 ==About this Structure==
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 [[Category: N-acetylglucosamibe]]
 [[Category: O-glcnacase]]
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