9NU4
Structure of MurJ in complex with single gene lysis protein from phage M
Summary for 9NU4
| Entry DOI | 10.2210/pdb9nu4/pdb |
| EMDB information | 49796 |
| Descriptor | Lipid II flippase MurJ, Lysis protein (2 entities in total) |
| Functional Keywords | lipid ii flippase, phage single gene lysis proteins, peptidoglycan biosynthesis, transport protein |
| Biological source | Escherichia coli K-12 More |
| Total number of polymer chains | 2 |
| Total formula weight | 73294.00 |
| Authors | Li, Y.E.,Clemons, W.M. (deposition date: 2025-03-19, release date: 2026-02-11, Last modification date: 2026-03-11) |
| Primary citation | Li, Y.E.,Antillon, S.F.,Baron, G.F.,Chamakura, K.,Young, R.,Clemons Jr., W.M. Convergent MurJ flippase inhibition by phage lysis proteins. Nature, 2026 Cited by PubMed Abstract: Antimicrobial drug resistance poses a global health challenge that necessitates the identification of new druggable targets. The essential lipid II flippase MurJ is a promising yet underexplored antimicrobial target in bacterial cell wall biosynthesis. The only known inhibitors of Gram-negative (diderm) MurJ are the single-gene lysis proteins (Sgls) from the lytic single-strand RNA phages M (Sgl) and PP7 (Sgl). Sgl and Sgl have distinct evolutionary origins and share no sequence similarity. Here we describe a common mechanism of MurJ inhibition by these phage-encoded Sgls. We determined the structures of MurJ-bound Sgl and Sgl and discovered a third distinct MurJ-targeting Sgl from the predicted phage Changjiang3 (Sgl) that we also characterized structurally. Our findings demonstrate that all three Sgls evolved convergently to trap MurJ in a periplasm-open conformation through a common MurJ interface, revealing a pathway for drug design. PubMed: 41741639DOI: 10.1038/s41586-026-10163-w PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (3.6 Å) |
Structure validation
Download full validation report
