8V33

Crystal structure of S. aureus TarL N-terminal domain

8V33 の概要

• エントリーDOI: 10.2210/pdb8v33/pdb
• 分子名称: Teichoic acid ribitol-phosphate polymerase TarL, SUCCINIC ACID (3 entities in total)
• 機能のキーワード: glycosyltransferase, immunoglobulin-like domain, transferase
• 由来する生物種: Staphylococcus aureus
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 22311.88

構造登録者

Li, F.K.K.,Strynadka, N.C.J. (登録日: 2023-11-26, 公開日: 2024-04-03)

主引用文献

Li, F.K.K.,Worrall, L.J.,Gale, R.T.,Brown, E.D.,Strynadka, N.C.J.
Cryo-EM analysis of S. aureus TarL, a polymerase in wall teichoic acid biogenesis central to virulence and antibiotic resistance.
Sci Adv, 10:eadj3864-eadj3864, 2024

PubMed Abstract: Wall teichoic acid (WTA), a covalent adduct of Gram-positive bacterial cell wall peptidoglycan, contributes directly to virulence and antibiotic resistance in pathogenic species. Polymerization of the WTA ribitol-phosphate chain is catalyzed by TarL, a member of the largely uncharacterized TagF-like family of membrane-associated enzymes. We report the cryo-electron microscopy structure of TarL, showing a tetramer that forms an extensive membrane-binding platform of monotopic helices. TarL is composed of an amino-terminal immunoglobulin-like domain and a carboxyl-terminal glycosyltransferase-B domain for ribitol-phosphate polymerization. The active site of the latter is complexed to donor substrate cytidine diphosphate-ribitol, providing mechanistic insights into the catalyzed phosphotransfer reaction. Furthermore, the active site is surrounded by electropositive residues that serve to retain the lipid-linked acceptor for polymerization. Our data advance general insight into the architecture and membrane association of the still poorly characterized monotopic membrane protein class and present molecular details of ribitol-phosphate polymerization that may aid in the design of new antimicrobials.

PubMed: 38416829
DOI: 10.1126/sciadv.adj3864

実験手法

X-RAY DIFFRACTION (1.7 Å)