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Structure and mechanism of a bacterial beta-glucosaminidase having O-GlcNAcase activity

Academic Article
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Overview

authors

  • Dennis, R. J.
  • Taylor, E. J.
  • Macauley, Matthew
  • Stubbs, K. A.
  • Turkenburg, J. P.
  • Hart, S. J.
  • Black, G. N.
  • Vocadlo, D. J.
  • Davies, G. J.

publication date

  • April 2006

journal

  • Nature Structural & Molecular Biology  Journal

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.

subject areas

  • Acetylglucosaminidase
  • Bacteroides
  • Base Sequence
  • Catalytic Domain
  • Cloning, Molecular
  • Crystallography, X-Ray
  • DNA, Bacterial
  • Hexosaminidases
  • Histone Acetyltransferases
  • Humans
  • Kinetics
  • Models, Molecular
  • Multienzyme Complexes
  • Mutagenesis, Site-Directed
  • Protein Conformation
  • Protein Processing, Post-Translational
  • Recombinant Proteins
  • Species Specificity
  • beta-N-Acetylhexosaminidases
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Identity

International Standard Serial Number (ISSN)

  • 1545-9985

Digital Object Identifier (DOI)

  • 10.1038/nsmb1079

PubMed ID

  • 16565725
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Additional Document Info

start page

  • 365

end page

  • 371

volume

  • 13

issue

  • 4

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