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Structure of the Wall Teichoic Acid Polymerase TagF, H444N variant
Structural highlights
FunctionTAGF_STAEQ Responsible for the polymerization of the main chain of the major teichoic acid by sequential transfer of glycerol phosphate units from CDP-glycerol to the disaccharide linkage unit. Synthesizes polymers of approximately 35 glycerol phosphate units in length.[1] Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedTeichoic 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. Structure of the bacterial teichoic acid polymerase TagF provides insights into membrane association and catalysis.,Lovering AL, Lin LY, Sewell EW, Spreter T, Brown ED, Strynadka NC Nat Struct Mol Biol. 2010 May;17(5):582-9. Epub 2010 Apr 18. PMID:20400947[2] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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