Structure and mechanism of Staphylococcus aureus TarM, the wall teichoic acid α-glycosyltransferase Academic Article uri icon

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  • Significance This paper describes the structure of Staphylococcus aureus TarM, an enzyme responsible for the glycosylation of wall teichoic acid that is important in pathological processes such as host immunity, phage binding, and antibiotic resistance in strains such as Methicillin-resistant S. aureus . The TarM structure is presented in an unusual ternary-like complex that features a polymeric acceptor substrate analogue and a trapped product of enzyme action, lending novel structural and mechanistic insight into the glycosylation of glycopolymers. More generally, the positioning of this product in the active site as well as the distorted conformation of its pyranose ring provide direct structural evidence for an internal substitution-like catalytic mechanism for retaining GT-B class enzymes.


  • Sobhanifar, Solmaz
  • Worrall, Liam James
  • Gruninger, Robert J
  • Wasney, Gregory A
  • Blaukopf, Markus
  • Baumann, Lars
  • Lameignere, Emilie
  • Solomonson, Matthew
  • Brown, Eric
  • Withers, Stephen G
  • Strynadka, Natalie CJ

publication date

  • February 10, 2015