11XX
Staphylococcus aureus MurJ in the outward-facing conformation
Summary for 11XX
| Entry DOI | 10.2210/pdb11xx/pdb |
| EMDB information | 76175 |
| Descriptor | Polysaccharide biosynthesis protein, putative (1 entity in total) |
| Functional Keywords | lipid ii flippase, peptidoglycan biosynthesis, transport protein |
| Biological source | Staphylococcus aureus (strain NCTC 8325 / PS 47) |
| Total number of polymer chains | 1 |
| Total formula weight | 61998.31 |
| Authors | |
| Primary citation | Li, Y.E.,Baron, G.F.,Clemons Jr., W.M. Structures of the lipid II flippase from the monoderm pathogen Staphylococcus aureus. J.Biol.Chem., :113516-113516, 2026 Cited by PubMed Abstract: Peptidoglycan biogenesis requires membrane flippases to translocate lipid-linked precursors across the cytoplasmic membrane for processing. This essential step is mediated by MurJ, the lipid II flippase conserved across all peptidoglycan-producing bacteria. While MurJ from diderm bacteria has been structurally resolved in multiple conformational states, its monoderm homolog remains uncharacterized. Monoderm MurJ homologs exhibit substantial sequence divergence yet retain the same lipid II flipping function and are promising antibiotic targets. Here we report structures of Staphylococcus aureus MurJ (SaMurJ) captured in both outward- and inward-facing conformations. These structures show that SaMurJ adopts the conserved MOP family fold and undergoes conformational transitions consistent with an alternating-access mechanism. Our findings reveal conserved and divergent features of MurJ between diderm and monoderm bacteria that are critical for lipid II flipping and provide a structural framework for probing substrate recognition and specific inhibition. PubMed: 42700959DOI: 10.1016/j.jbc.2026.113516 PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (3.6 Å) |
Structure validation
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