9M3L
Crystal structure of ADP-ribosylated endolytic muramidase TdeM from Pseudomonas aeruginosa
Summary for 9M3L
| Entry DOI | 10.2210/pdb9m3l/pdb |
| Descriptor | ADP-ribosylated endolytic muramidase TdeM, BENZAMIDINE, ZINC ION, ... (4 entities in total) |
| Functional Keywords | adp-ribosylated endolytic muramidase tdem, de novo protein |
| Biological source | Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1) |
| Total number of polymer chains | 2 |
| Total formula weight | 43318.81 |
| Authors | |
| Primary citation | Wang, T.,Zhang, L.,Lee, M.,Yan, W.,Liu, Q.,Wang, C.,Feltzer, R.,Hesek, D.,Mobashery, S.,Zhang, L.,Liang, H. A Pseudomonas aeruginosa endolytic muramidase targets cell-wall peptidoglycan in bacterial competition. J.Biol.Chem., 301:110642-110642, 2025 Cited by PubMed Abstract: Pseudomonas aeruginosa is an opportunistic pathogen that frequently resides in multispecies communities. During chronic infections, P. aeruginosa employs a diverse arsenal of antibacterial weapons to compete with other bacteria for resources and space. Using genetic and biochemical approaches, we identified a type VI secretion system-dependent antibacterial effector-immunity pair, PseM (P. aeruginosa secreted endolytic muramidase) and PA0990 in P. aeruginosa. Our findings demonstrate that PseM functions as an endolytic muramidase, targeting prey bacteria by hydrolytically cleaving cell-wall peptidoglycan, whereas its immunity partner PA0990 provides self-protection. The X-ray crystal structure of PseM reveals a homodimeric configuration, with its active site formed by segments from both monomers. Through structural analysis and macromolecular docking simulations, we further elucidate the substrate-binding residues critical for the activity of PseM. Importantly, we show that PseM contributes to P. aeruginosa growth among bacterial competition. Together, these results uncover a novel antibacterial mechanism mediated by PseM, highlighting the dynamic nature of interspecies and intraspecies competition within bacterial populations. PubMed: 40885384DOI: 10.1016/j.jbc.2025.110642 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2 Å) |
Structure validation
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