7BWL

Structure of antibiotic sequester from Pseudomonas aerurinosa

7BWL の概要

• エントリーDOI: 10.2210/pdb7bwl/pdb
• 分子名称: UPF0312 protein PA0423, Ubiquinone-8 (3 entities in total)
• 機能のキーワード: lipocalin family, antibiotic sequester, antibiotic resistance, antibiotic
• 由来する生物種: Pseudomonas aeruginosa PAO1
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 21530.47

構造登録者

Hong, M. (登録日: 2020-04-14, 公開日: 2020-12-02, 最終更新日: 2023-11-29)

主引用文献

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

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: 32451086
DOI: 10.1016/j.bbrc.2020.05.023

実験手法

X-RAY DIFFRACTION (2.25 Å)