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Crystal structure of PilF: functional implication in the type 4 pilus biogenesis in Pseudomonas aeruginosa
Kyunggon Kim1, Jongkil Oh, Dohyun Han
1Division of Molecular Genomic Medicine, College of Medicine, Seoul National University, Yongon-Dong, Seoul 110-799, Republic of Korea.
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.
Insights
The structure of PilF protein from Pseudomonas aeruginosa was determined, revealing its role in type 4 pilus biogenesis. PilF may act as a bridgehead, interacting with other essential proteins like PilG, PilU, PilY, and PilZ.
Area of Science:
- Microbiology
- Structural Biology
- Bacterial Pathogenesis
Background:
- PilF is essential for type 4 pilus assembly in Pseudomonas aeruginosa, a significant human pathogen.
- Type 4 pili are crucial for bacterial adhesion, motility, and DNA uptake.
Purpose of the Study:
- To elucidate the three-dimensional structure of the PilF protein.
- To identify potential binding partners of PilF within the type 4 pilus biogenesis pathway.
Main Methods:
- X-ray crystallography was used to determine the PilF structure at 2.2Å resolution.
- In silico screening was performed to identify potential PilF-interacting peptides.
Main Results:
- The PilF structure comprises six tandem tetratrico peptide repeat (TPR) units forming a right-handed superhelix.
- PilF shares structural similarity with heat shock protein organizing proteins, suggesting a conserved interaction mechanism.
- Simulated screening identified C-terminal pentapeptides of PilG, PilU, PilY, and PilZ as likely PilF binders.
Conclusions:
- PilF's structure suggests it functions as a crucial bridgehead protein in protein-protein interactions.
- PilF likely plays a key role in mediating interactions with other components of the type 4 pilus biogenesis system, such as PilG, PilU, PilY, and PilZ.
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