Download MendeleyCrystal structure of the Pseudomonas aeruginosa PA0423 protein and its functional implication in antibiotic sequestration.
Lee, C., Kim, M.I., Park, J., Kim, J., Oh, H., Cho, Y., Son, J., Jeon, B.Y., Ka, H., Hong, M.(2020) Biochem Biophys Res Commun 528: 85-91
- PubMed: 32451086
- DOI: https://doi.org/10.1016/j.bbrc.2020.05.023
- Primary Citation of Related Structures:
7BWL - PubMed Abstract:
Pseudomonas aeruginosa is a widely found opportunistic pathogen. The emergence of multidrug-resistant strains and persistent chronic infections have increased. The protein encoded by the pa0423 gene in P. aeruginosa is proposed to be critical for pathogenesis and could be a virulence-promoting protease or a bacterial lipocalin that binds a lipid-like antibiotic for drug resistance. Although two functions of proteolysis and antibiotic resistance are mutually related to bacterial survival in the host, it is very unusual for a single-domain protein to target unrelated ligand molecules such as protein substrates and lipid-like antibiotics. To clearly address the biological role of the PA0423 protein, we performed structural and biochemical studies. We found that PA0423 adopts a single-domain β-barrel structure and belongs to the lipocalin family. The PA0423 structure houses an internal tubular cavity, which accommodates a ubiquinone-8 molecule. Furthermore, we reveal that PA0423 can directly interact with the polymyxin B antibiotic using the internal cavity, suggesting that PA0423 has a physiological function in the antibiotic resistance of P. aeruginosa.
Organizational Affiliation:
Division of Biological Science and Technology, Yonsei University, Wonju 26493, Republic of Korea.
