S-Space College of Medicine/School of Medicine (의과대학/대학원) Molecular and Genomic Medicine (분자유전체의학전공) Journal Papers (저널논문_분자유전체의학전공)
Crystal structure of PilF: functional implication in the type 4 pilus biogenesis in Pseudomonas aeruginosa
- Kim, Kyunggon; Oh, Jongkil; Han, Dohyun; Kim, Eunice EunKyeong; Lee, Byungil; Kim, Youngsoo
- Issue Date
- Biochem Biophys Res Commun. 2006 Feb 24;340(4):1028-38. Epub 2005 Dec 27.
- Amino Acid Sequence; Binding Sites; Biogenesis; Computer Simulation; Crystallography; Dimerization; Fimbriae Proteins/*chemistry/metabolism/*ultrastructure; Fimbriae, Bacterial/*chemistry/physiology/ultrastructure; Models, Biological; *Models, Molecular; Molecular Sequence Data; Multiprotein Complexes/chemistry/ultrastructure; Protein Binding; Protein Conformation; Pseudomonas aeruginosa/*chemistry/growth & development/ultrastructure; Structure-Activity Relationship
- 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.
- 0006-291X (Print)
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