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8TUM

Type IV pilus from Pseudomonas PAO1 strain

Summary for 8TUM
Entry DOI10.2210/pdb8tum/pdb
EMDB information41625 41780
DescriptorType IV major pilin protein PilA (1 entity in total)
Functional Keywordstype iv pilus, t4p, pao1, membrane protein
Biological sourcePseudomonas aeruginosa PAO1
Total number of polymer chains16
Total formula weight238062.22
Authors
Thongchol, J.,Zhang, J.,Zeng, L. (deposition date: 2023-08-16, release date: 2024-03-13, Last modification date: 2024-10-23)
Primary citationThongchol, 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: 38574145
DOI: 10.1126/science.adl0635
PDB entries with the same primary citation
Experimental method
ELECTRON MICROSCOPY (3.6 Å)
Structure validation

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数据于2024-11-06公开中

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