2cho
From Proteopedia
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==Overview== | ==Overview== | ||
| - | O-GlcNAc is an abundant post-translational modification of serine and | + | 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== | ==About this Structure== | ||
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[[Category: Beta-N-acetylhexosaminidase]] | [[Category: Beta-N-acetylhexosaminidase]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
| - | [[Category: Black, G | + | [[Category: Black, G N.]] |
| - | [[Category: Davies, G | + | [[Category: Davies, G J.]] |
| - | [[Category: Dennis, R | + | [[Category: Dennis, R J.]] |
| - | [[Category: Hart, S | + | [[Category: Hart, S J.]] |
| - | [[Category: Macauley, M | + | [[Category: Macauley, M S.]] |
| - | [[Category: Stubbs, K | + | [[Category: Stubbs, K A.]] |
| - | [[Category: Taylor, E | + | [[Category: Taylor, E J.]] |
| - | [[Category: Turkenburg, J | + | [[Category: Turkenburg, J P.]] |
| - | [[Category: Vocadlo, D | + | [[Category: Vocadlo, D J.]] |
[[Category: ACT]] | [[Category: ACT]] | ||
[[Category: CA]] | [[Category: CA]] | ||
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[[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 Thu Feb 21 16:48:44 2008'' |
Revision as of 14:48, 21 February 2008
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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 with , and as ligands. Active as Beta-N-acetylhexosaminidase, with EC number 3.2.1.52 Known structural/functional Site: . 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
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