3L7J

Structure of the Wall Teichoic Acid Polymerase TagF, H444N variant

3L7J の概要

• エントリーDOI: 10.2210/pdb3l7j/pdb
• 関連するPDBエントリー: 3L7I 3L7K 3L7L 3L7M
• 分子名称: Teichoic acid biosynthesis protein F, SULFATE ION, CHLORIDE ION, ... (4 entities in total)
• 機能のキーワード: gt-b, monotopic membrane protein, structural protein
• 由来する生物種: Staphylococcus epidermidis
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 349947.41

構造登録者

Strynadka, N.C.J.,Lovering, A.L. (登録日: 2009-12-28, 公開日: 2010-04-28, 最終更新日: 2023-09-06)

主引用文献

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

実験手法

X-RAY DIFFRACTION (2.81 Å)