8TUX
Capsid of mature PP7 virion with 3'end region of PP7 genomic RNA
This is a non-PDB format compatible entry.
Summary for 8TUX
| Entry DOI | 10.2210/pdb8tux/pdb |
| EMDB information | 41632 |
| Descriptor | 3'end of PP7 genomic RNA, Maturation protein A, Capsid protein (3 entities in total) |
| Functional Keywords | maturation protein, pp7, pepevirus, viral protein |
| Biological source | Pseudomonas phage PP7 More |
| Total number of polymer chains | 181 |
| Total formula weight | 2607395.94 |
| Authors | Thongchol, J.,Zhang, J.,Zeng, L. (deposition date: 2023-08-17, release date: 2024-03-13, Last modification date: 2024-10-30) |
| Primary citation | Thongchol, J.,Yu, Z.,Harb, L.,Lin, Y.,Koch, M.,Theodore, M.,Narsaria, U.,Shaevitz, J.,Gitai, Z.,Wu, Y.,Zhang, J.,Zeng, L. Removal of Pseudomonas type IV pili by a small RNA virus. Science, 384:eadl0635-eadl0635, 2024 Cited by PubMed Abstract: The retractile type IV pilus (T4P) is important for virulence of the opportunistic human pathogen . The single-stranded RNA (ssRNA) phage PP7 binds to T4P and is brought to the cell surface through pilus retraction. Using fluorescence microscopy, we discovered that PP7 detaches T4P, which impairs cell motility and restricts the pathogen's virulence. Using cryo-electron microscopy, mutagenesis, optical trapping, and Langevin dynamics simulation, we resolved the structure of PP7, T4P, and the PP7/T4P complex and showed that T4P detachment is driven by the affinity between the phage maturation protein and its bound pilin, plus the pilus retraction force and speed, and pilus bending. Pilus detachment may be widespread among other ssRNA phages and their retractile pilus systems and offers new prospects for antibacterial prophylaxis and therapeutics. PubMed: 38574145DOI: 10.1126/science.adl0635 PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (3.9 Å) |
Structure validation
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