2cho
BACTEROIDES THETAIOTAOMICRON HEXOSAMINIDASE WITH O-GLCNACASE ACTIVITY
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OverviewOverview
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 StructureAbout this Structure
2CHO is a Single protein structure of sequence from Bacteroides thetaiotaomicron with CA, ACT and GOL as ligands. Active as Beta-N-acetylhexosaminidase, with EC number 3.2.1.52 Structure known Active Site: AC1. 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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