Summary for 7QD7
| Entry DOI | 10.2210/pdb7qd7/pdb |
| Descriptor | TarM(Se)_G117R, CHLORIDE ION, PHOSPHATE ION, ... (6 entities in total) |
| Functional Keywords | staphylococcus epidermidis, glycosyltransferase, gt-b fold, alpha-o-glucose, wall teichoic acid, transferase |
| Biological source | Escherichia coli BL21(DE3) |
| Total number of polymer chains | 1 |
| Total formula weight | 60457.93 |
| Authors | Guo, Y.,Stehle, T. (deposition date: 2021-11-26, release date: 2023-05-10, Last modification date: 2023-12-06) |
| Primary citation | Guo, Y.,Du, X.,Krusche, J.,Beck, C.,Ali, S.,Walter, A.,Winstel, V.,Mayer, C.,Codee, J.D.C.,Peschel, A.,Stehle, T. Invasive Staphylococcus epidermidis uses a unique processive wall teichoic acid glycosyltransferase to evade immune recognition. Sci Adv, 9:eadj2641-eadj2641, 2023 Cited by PubMed Abstract: expresses glycerol phosphate wall teichoic acid (WTA), but some health care-associated methicillin-resistant (HA-MRSE) clones produce a second, ribitol phosphate (RboP) WTA, resembling that of the aggressive pathogen . RboP-WTA promotes HA-MRSE persistence and virulence in bloodstream infections. We report here that the TarM enzyme of HA-MRSE [TarM(Se)] glycosylates RboP-WTA with glucose, instead of -acetylglucosamine (GlcNAc) by TarM(Sa) in . Replacement of GlcNAc with glucose in RboP-WTA impairs HA-MRSE detection by human immunoglobulin G, which may contribute to the immune-evasion capacities of many invasive . Crystal structures of complexes with uridine diphosphate glucose (UDP-glucose), and with UDP and glycosylated poly(RboP), reveal the binding mode and glycosylation mechanism of this enzyme and explain why TarM(Se) and TarM(Sa) link different sugars to poly(RboP). These structural data provide evidence that TarM(Se) is a processive WTA glycosyltransferase. Our study will support the targeted inhibition of TarM enzymes, and the development of RboP-WTA targeting vaccines and phage therapies. PubMed: 38000019DOI: 10.1126/sciadv.adj2641 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.06 Å) |
Structure validation
Download full validation report
