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Structure and mechanism of a bacterial β-glucosaminidase having O-GlcNAcase activity.
- Source :
- Nature Structural & Molecular Biology; Apr2006, Vol. 13 Issue 4, p365-371, 7p
- Publication Year :
- 2006
-
Abstract
- 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. [ABSTRACT FROM AUTHOR]
- Subjects :
- PROTEINS
PHOSPHORYLATION
PHOSPHATASES
GLYCOSIDASES
ENZYMES
Subjects
Details
- Language :
- English
- ISSN :
- 15459993
- Volume :
- 13
- Issue :
- 4
- Database :
- Complementary Index
- Journal :
- Nature Structural & Molecular Biology
- Publication Type :
- Academic Journal
- Accession number :
- 20927831
- Full Text :
- https://doi.org/10.1038/nsmb1079