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-Structure paper
タイトル | Cryo-EM analysis of TarL, a polymerase in wall teichoic acid biogenesis central to virulence and antibiotic resistance. |
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ジャーナル・号・ページ | Sci Adv, Vol. 10, Issue 9, Page eadj3864, Year 2024 |
掲載日 | 2024年2月28日 |
![]() | Franco K K Li / Liam J Worrall / Robert T Gale / Eric D Brown / Natalie C J Strynadka / ![]() |
PubMed 要旨 | 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 ...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. |
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手法 | EM (単粒子) / X線回折 |
解像度 | 1.7 - 3.7 Å |
構造データ | EMDB-43083, PDB-8va1: ![]() EMDB-43084: S. aureus TarL H300N in complex with CDP-ribitol (two tetramers with CHAPS micelle) ![]() PDB-8v33: ![]() PDB-8v34: |
化合物 | ![]() ChemComp-SIN: ![]() ChemComp-HOH: ![]() ChemComp-V2V: |
由来 |
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![]() | TRANSFERASE / glycosyltransferase / immunoglobulin-like domain / polymerase / monotopic / amphipathic |