2cho

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[[Image:2cho.gif|left|200px]]
[[Image:2cho.gif|left|200px]]
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{{Structure
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<!--
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|PDB= 2cho |SIZE=350|CAPTION= <scene name='initialview01'>2cho</scene>, resolution 1.85&Aring;
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The line below this paragraph, containing "STRUCTURE_2cho", creates the "Structure Box" on the page.
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|SITE= <scene name='pdbsite=AC1:Gol+Binding+Site+For+Chain+B'>AC1</scene>
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You may change the PDB parameter (which sets the PDB file loaded into the applet)
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|LIGAND= <scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene>, <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=UNK:UNKNOWN'>UNK</scene>
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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|ACTIVITY= <span class='plainlinks'>[http://en.wikipedia.org/wiki/Beta-N-acetylhexosaminidase Beta-N-acetylhexosaminidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.2.1.52 3.2.1.52] </span>
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or leave the SCENE parameter empty for the default display.
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|GENE=
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-->
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|DOMAIN=
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{{STRUCTURE_2cho| PDB=2cho | SCENE= }}
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|RELATEDENTRY=
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2cho FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2cho OCA], [http://www.ebi.ac.uk/pdbsum/2cho PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=2cho RCSB]</span>
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}}
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'''BACTEROIDES THETAIOTAOMICRON HEXOSAMINIDASE WITH O-GLCNACASE ACTIVITY'''
'''BACTEROIDES THETAIOTAOMICRON HEXOSAMINIDASE WITH O-GLCNACASE ACTIVITY'''
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[[Category: Turkenburg, J P.]]
[[Category: Turkenburg, J P.]]
[[Category: Vocadlo, D J.]]
[[Category: Vocadlo, D J.]]
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[[Category: hydrolase]]
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[[Category: Hydrolase]]
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[[Category: n-acetylglucosamine]]
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[[Category: N-acetylglucosamine]]
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[[Category: o-glcnacase]]
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[[Category: O-glcnacase]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 22:09:47 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 02:21:35 2008''
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Revision as of 19:09, 3 May 2008

Image:2cho.gif

Template:STRUCTURE 2cho

BACTEROIDES THETAIOTAOMICRON HEXOSAMINIDASE WITH O-GLCNACASE ACTIVITY


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.

About this Structure

2CHO is a Single protein structure of sequence from Bacteroides thetaiotaomicron. Full crystallographic information is available from OCA.

Reference

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 Page seeded by OCA on Sat May 3 22:09:47 2008

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