3L7I

Structure of the Wall Teichoic Acid Polymerase TagF

Summary for 3L7I

• Entry DOI: 10.2210/pdb3l7i/pdb
• Related: 3L7J 3L7K 3L7L 3L7M
• Descriptor: Teichoic acid biosynthesis protein F, SULFATE ION, CHLORIDE ION, ... (5 entities in total)
• Functional Keywords: gt-b fold, monotopic membrane protein, structural protein
• Biological source: Staphylococcus epidermidis
• Total number of polymer chains: 4
• Total formula weight: 350141.19

Authors

Strynadka, N.C.J.,Lovering, A.L. (deposition date: 2009-12-28, release date: 2010-04-28, Last modification date: 2024-02-21)

Primary citation

Lovering, A.L.,Lin, L.Y.,Sewell, E.W.,Spreter, T.,Brown, E.D.,Strynadka, N.C.
Structure of the bacterial teichoic acid polymerase TagF provides insights into membrane association and catalysis.
Nat.Struct.Mol.Biol., 17:582-589, 2010

PubMed 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.

PubMed: 20400947
DOI: 10.1038/nsmb.1819

Experimental method

X-RAY DIFFRACTION (2.7 Å)