Structure of the bacterial teichoic acid polymerase TagF provides insights into membrane association and catalysis Academic Article uri icon

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abstract

  • Teichoic acid polymers are composed of polyol-phosphate units and form a major component of Gram-positive bacterial cell walls. These anionic compounds perform a multitude of important roles in bacteria and are synthesized by monotopic membrane proteins of the TagF polymerase family. We have determined the structure of Staphylococcus epidermidis TagF to 2.7-A resolution from a construct that includes both the membrane-targeting region and the glycerol-phosphate polymerase domains. TagF possesses a helical region for interaction with the lipid bilayer, placing the active site at a suitable distance for access to the membrane-bound substrate. Characterization of active-site residue variants and analysis of a CDP-glycerol substrate complex suggest a mechanism for polymer synthesis. With the importance of teichoic acid in Gram-positive physiology, this elucidation of the molecular details of TagF function provides a critical new target in the development of novel anti-infectives.

authors

  • Lovering, Andrew L
  • Lin, Leo Y-C
  • Sewell, Edward W
  • Spreter, Thomas
  • Brown, Eric
  • Strynadka, Natalie CJ

publication date

  • May 2010