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TitleCryo-EM analysis of TarL, a polymerase in wall teichoic acid biogenesis central to virulence and antibiotic resistance.
Journal, issue, pagesSci Adv, Vol. 10, Issue 9, Page eadj3864, Year 2024
Publish dateFeb 28, 2024
AuthorsFranco K K Li / Liam J Worrall / Robert T Gale / Eric D Brown / Natalie C J Strynadka /
PubMed AbstractWall 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.
External linksSci Adv / PubMed:38416829 / PubMed Central
MethodsEM (single particle) / X-ray diffraction
Resolution1.7 - 3.7 Å
Structure data

43083

8va1

EMDB-43083, PDB-8va1:
S. aureus TarL H300N in complex with CDP-ribitol (single tetramer)
Method: EM (single particle) / Resolution: 3.4 Å

EMDB-43084: S. aureus TarL H300N in complex with CDP-ribitol (two tetramers with CHAPS micelle)
Method: EM (single particle) / Resolution: 3.7 Å

PDB-8v33:
Crystal structure of S. aureus TarL N-terminal domain
Method: X-RAY DIFFRACTION / Resolution: 1.7 Å

PDB-8v34:
Crystal structure of S. aureus TarK N-terminal domain
Method: X-RAY DIFFRACTION / Resolution: 3 Å

Chemicals

ChemComp-SIN:
SUCCINIC ACID

ChemComp-HOH:
WATER

ChemComp-V2V:
CDP-ribitol

Source
  • staphylococcus aureus (bacteria)
KeywordsTRANSFERASE / glycosyltransferase / immunoglobulin-like domain / polymerase / monotopic / amphipathic

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