7BWL
Structure of antibiotic sequester from Pseudomonas aerurinosa
Summary for 7BWL
| Entry DOI | 10.2210/pdb7bwl/pdb |
| Descriptor | UPF0312 protein PA0423, Ubiquinone-8 (3 entities in total) |
| Functional Keywords | lipocalin family, antibiotic sequester, antibiotic resistance, antibiotic |
| Biological source | Pseudomonas aeruginosa PAO1 |
| Total number of polymer chains | 1 |
| Total formula weight | 21530.47 |
| Authors | Hong, M. (deposition date: 2020-04-14, release date: 2020-12-02, Last modification date: 2023-11-29) |
| Primary citation | Lee, C.,Kim, M.I.,Park, J.,Kim, J.,Oh, H.,Cho, Y.,Son, J.,Jeon, B.Y.,Ka, H.,Hong, M. Crystal structure of the Pseudomonas aeruginosa PA0423 protein and its functional implication in antibiotic sequestration. Biochem.Biophys.Res.Commun., 528:85-91, 2020 Cited by 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. PubMed: 32451086DOI: 10.1016/j.bbrc.2020.05.023 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.25 Å) |
Structure validation
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