Structure and mechanism ofStaphylococcus aureusTarM, the wall teichoic acid α-glycosyltransferase Journal Articles uri icon

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  • SignificanceThis paper describes the structure ofStaphylococcus aureusTarM, 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-resistantS. 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