8TUW
Type IV pilus from Pseudomonas PAO1 strain with PP7 Maturation protein
This is a non-PDB format compatible entry.
Summary for 8TUW
| Entry DOI | 10.2210/pdb8tuw/pdb |
| EMDB information | 41633 41780 |
| Descriptor | Maturation protein A, Type IV major pilin protein PilA (2 entities in total) |
| Functional Keywords | type iv pilus, t4p, pao1, membrane protein |
| Biological source | Pseudomonas aeruginosa PAO1 More |
| Total number of polymer chains | 17 |
| Total formula weight | 288825.99 |
| Authors | Thongchol, J.,Zhang, J.,Zeng, L. (deposition date: 2023-08-17, release date: 2024-03-13, Last modification date: 2024-11-13) |
| 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 (7.9 Å) |
Structure validation
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