Summary for 9RKT
| Entry DOI | 10.2210/pdb9rkt/pdb |
| EMDB information | 54020 |
| Descriptor | Structural protein (1 entity in total) |
| Functional Keywords | flagella phage, agrobacterium sp. h13-3, collar, virus |
| Biological source | Agrobacterium phage 7-7-1 |
| Total number of polymer chains | 60 |
| Total formula weight | 1491231.00 |
| Authors | Noteborn, W.E.M.,Hoeksma, T.,Briegel, A. (deposition date: 2025-06-14, release date: 2025-12-10, Last modification date: 2026-01-21) |
| Primary citation | Noteborn, W.E.M.,Ouyang, R.,Hoeksma, T.,Sidi Mabrouk, A.,Esteves, N.C.,Pelt, D.M.,Scharf, B.E.,Briegel, A. Insights into the structure and initial host attachment of the flagellotropic bacteriophage 7-7-1. Commun Biol, 9:55-55, 2025 Cited by PubMed Abstract: Understanding the structural and functional mechanisms of bacteriophage 7-7-1, the flagellotropic phage infecting Agrobacterium sp. H13-3, offers promising insights into phage-host interactions. Using single particle analysis (SPA) cryo-electron microscopy (cryo-EM), we determined the capsid, neck region, tail, and baseplate complex structures. Combined with cryo-electron tomography (cryo-ET) and machine learning methodologies, our findings indicate that phage 7-7-1 uses capsid fibers to establish initial contact with the host flagellum, followed by subsequent attachment to cell surface receptors. The study also demonstrated that capsid fibers are flexible and can interact with other phages and host flagella, suggesting a cooperative infection strategy. These results provide crucial structural insights and may open avenues for developing phage-based therapeutics against resistant bacterial pathogens. PubMed: 41353512DOI: 10.1038/s42003-025-09319-7 PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (3.31 Å) |
Structure validation
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