Membrane association of monotopic phosphoglycosyl transferase underpins function

Nat Chem Biol. 2018 Jun;14(6):538-541. doi: 10.1038/s41589-018-0054-z. Epub 2018 May 16.

Abstract

Polyprenol phosphate phosphoglycosyl transferases (PGTs) catalyze the first membrane-committed step in assembly of essential glycoconjugates. Currently there is no structure-function information to describe how monotopic PGTs coordinate the reaction between membrane-embedded and soluble substrates. We describe the structure and mode of membrane association of PglC, a PGT from Campylobacter concisus. The structure reveals a unique architecture, provides mechanistic insight and identifies ligand-binding determinants for PglC and the monotopic PGT superfamily.

Publication types

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

MeSH terms

  • Campylobacter / enzymology*
  • Catalysis
  • Catalytic Domain
  • Cell Membrane / enzymology*
  • Cloning, Molecular
  • Cysteine / chemistry
  • Glycoconjugates / chemistry
  • Glycosyltransferases / chemistry*
  • Ligands
  • Mutation
  • Phosphates / chemistry*
  • Phosphorylation
  • Protein Domains
  • Protein Folding
  • Protein Structure, Secondary
  • Structure-Activity Relationship
  • Substrate Specificity

Substances

  • Glycoconjugates
  • Ligands
  • Phosphates
  • Glycosyltransferases
  • Cysteine