2cho
From Proteopedia
| Line 4: | Line 4: | ||
|PDB= 2cho |SIZE=350|CAPTION= <scene name='initialview01'>2cho</scene>, resolution 1.85Å | |PDB= 2cho |SIZE=350|CAPTION= <scene name='initialview01'>2cho</scene>, resolution 1.85Å | ||
|SITE= <scene name='pdbsite=AC1:Gol+Binding+Site+For+Chain+B'>AC1</scene> | |SITE= <scene name='pdbsite=AC1:Gol+Binding+Site+For+Chain+B'>AC1</scene> | ||
| - | |LIGAND= <scene name='pdbligand= | + | |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> |
| - | |ACTIVITY= [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] | + | |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> |
|GENE= | |GENE= | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY= | ||
| + | |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> | ||
}} | }} | ||
| Line 32: | Line 35: | ||
[[Category: Turkenburg, J P.]] | [[Category: Turkenburg, J P.]] | ||
[[Category: Vocadlo, D J.]] | [[Category: Vocadlo, D J.]] | ||
| - | [[Category: ACT]] | ||
| - | [[Category: CA]] | ||
| - | [[Category: GOL]] | ||
[[Category: hydrolase]] | [[Category: hydrolase]] | ||
[[Category: n-acetylglucosamine]] | [[Category: n-acetylglucosamine]] | ||
[[Category: o-glcnacase]] | [[Category: o-glcnacase]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 02:21:35 2008'' |
Revision as of 23:21, 30 March 2008
| |||||||
| , resolution 1.85Å | |||||||
|---|---|---|---|---|---|---|---|
| Sites: | |||||||
| Ligands: | , , , | ||||||
| Activity: | Beta-N-acetylhexosaminidase, with EC number 3.2.1.52 | ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
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 Mon Mar 31 02:21:35 2008
