8OWS
The crystal structure of the polymorphic toxin PT1(Em) H44A mutant and its cognate immunity PIM1(Em) complex
Summary for 8OWS
| Entry DOI | 10.2210/pdb8ows/pdb |
| Descriptor | PIM1, Type IV secretion protein Rhs (3 entities in total) |
| Functional Keywords | bacterial toxins, polymorphic toxins, antimicrobials, dnase., toxin |
| Biological source | Escherichia marmotae More |
| Total number of polymer chains | 2 |
| Total formula weight | 29605.85 |
| Authors | Tzarum, N.,Fraenkel, R.,Deouell, N.,Cahana, I. (deposition date: 2023-04-28, release date: 2024-07-03, Last modification date: 2024-11-13) |
| Primary citation | Nachmias, N.,Dotan, N.,Rocha, M.C.,Fraenkel, R.,Detert, K.,Kluzek, M.,Shalom, M.,Cheskis, S.,Peedikayil-Kurien, S.,Meitav, G.,Rivitz, A.,Shamash-Halevy, N.,Cahana, I.,Deouell, N.,Klein, J.,Oren-Suissa, M.,Schmidt, H.,Schlezinger, N.,Tzarum, N.,Oppenheimer-Shaanan, Y.,Levy, A. Systematic discovery of antibacterial and antifungal bacterial toxins. Nat Microbiol, 9:3041-3058, 2024 Cited by PubMed Abstract: Microorganisms use toxins to kill competing microorganisms or eukaryotic cells. Polymorphic toxins are proteins that encode carboxy-terminal toxin domains. Here we developed a computational approach to identify previously undiscovered, conserved toxin domains of polymorphic toxins within 105,438 microbial genomes. We validated nine short toxins, showing that they cause cell death upon heterologous expression in either Escherichia coli or Saccharomyces cerevisiae. Five cognate immunity genes that neutralize the toxins were also discovered. The toxins are encoded by 2.2% of sequenced bacteria. A subset of the toxins exhibited potent antifungal activity against various pathogenic fungi but not against two invertebrate model organisms or macrophages. Experimental validation suggested that these toxins probably target the cell membrane or DNA or inhibit cell division. Further characterization and structural analysis of two toxin-immunity protein complexes confirmed DNase activity. These findings expand our knowledge of microbial toxins involved in inter-microbial competition that may have the potential for clinical and biotechnological applications. PubMed: 39438720DOI: 10.1038/s41564-024-01820-9 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.39 Å) |
Structure validation
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