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Crystal structure of PilF: functional implication in the type 4 pilus biogenesis in Pseudomonas aeruginosa
Cited 47 time in
Web of Science
Cited 47 time in Scopus
- Authors
- Issue Date
- 2006-01-13
- Publisher
- Elsevier
- Citation
- Biochem Biophys Res Commun. 2006 Feb 24;340(4):1028-38. Epub 2005 Dec 27.
- Keywords
- Amino Acid Sequence ; Binding Sites ; Biogenesis ; Computer Simulation ; Crystallography ; Dimerization ; Fimbriae Proteins/*chemistry/metabolism/*ultrastructure ; Fimbriae, Bacterial/*chemistry/physiology/ultrastructure ; Models, Biological ; Molecular Sequence Data ; Multiprotein Complexes/chemistry/ultrastructure ; Protein Binding ; Protein Conformation ; Pseudomonas aeruginosa/*chemistry/growth & development/ultrastructure ; Structure-Activity Relationship ; Models, Molecular
- Abstract
- PilF is a requisite protein involved in the type 4 pilus biogenesis system from the Gram-negative human pathogenic bacteria, Pseudomonas aeruginosa. We determined the PilF structure at a 2.2A resolution; this includes six tandem tetratrico peptide repeat (TPR) units forming right-handed superhelix. PilF structure was similar to the heat shock protein organizing protein, which interacts with the C-terminal peptide of Hsp90 and Hsp70 via a concave Asn ladder in the inner groove of TPR superhelix. After simulated screening, the C-terminal pentapeptides of PilG, PilU, PilY, and PilZ proved to be a likely candidate binding to PilF, which are ones of 25 necessary components involved in the type 4 pilus biogenesis system. We proposed that PilF would be critical as a bridgehead in protein-protein interaction and thereby, PilF may bind a necessary molecule in type 4 pilus biogenesis system such as PilG, PilU, PilY, and PilZ.
- ISSN
- 0006-291X (Print)
- Language
- English
- URI
- http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&dopt=Citation&list_uids=16403447
https://hdl.handle.net/10371/39195
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