Structural snapshots of the reaction coordinate for O-GlcNAc transferase

Nat Chem Biol. 2012 Dec;8(12):966-8. doi: 10.1038/nchembio.1109. Epub 2012 Oct 28.

Abstract

Visualization of the reaction coordinate undertaken by glycosyltransferases has remained elusive but is critical for understanding this important class of enzyme. Using substrates and substrate mimics, we describe structural snapshots of all species along the kinetic pathway for human O-linked β-N-acetylglucosamine transferase (O-GlcNAc transferase), an intracellular enzyme that catalyzes installation of a dynamic post-translational modification. The structures reveal key features of the mechanism and show that substrate participation is important during catalysis.

Publication types

  • Research Support, N.I.H., Extramural
  • Research Support, Non-U.S. Gov't

MeSH terms

  • Catalysis
  • Crystallography, X-Ray
  • Glycosylation
  • Humans
  • Kinetics
  • Models, Molecular
  • Molecular Mimicry
  • N-Acetylglucosaminyltransferases / chemistry
  • N-Acetylglucosaminyltransferases / metabolism*
  • Protein Conformation
  • Protein Processing, Post-Translational
  • Substrate Specificity

Substances

  • N-Acetylglucosaminyltransferases
  • O-GlcNAc transferase

Associated data

  • PDB/4GYW
  • PDB/4GYY
  • PDB/4GZ3
  • PDB/4GZ5
  • PDB/4GZ6