8VA1
S. aureus TarL H300N in complex with CDP-ribitol (single tetramer)
Summary for 8VA1
| Entry DOI | 10.2210/pdb8va1/pdb |
| Related | 8V33 8V34 |
| EMDB information | 43083 |
| Descriptor | Teichoic acid ribitol-phosphate polymerase TarL, CDP-ribitol (2 entities in total) |
| Functional Keywords | glycosyltransferase, polymerase, monotopic, amphipathic, transferase |
| Biological source | Staphylococcus aureus |
| Total number of polymer chains | 4 |
| Total formula weight | 276192.04 |
| Authors | |
| Primary citation | 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 Cited by 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: 38416829DOI: 10.1126/sciadv.adj3864 PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (3.4 Å) |
Structure validation
Download full validation report
