Cited 3 times in
Crystal structure of the Pseudomonas aeruginosa PA0423 protein and its functional implication in antibiotic sequestration
DC Field | Value | Language |
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dc.date.accessioned | 2022-09-02T01:12:21Z | - |
dc.date.available | 2022-09-02T01:12:21Z | - |
dc.date.issued | 2020-07 | - |
dc.identifier.issn | 0006-291X | - |
dc.identifier.uri | https://ir.ymlib.yonsei.ac.kr/handle/22282913/190054 | - |
dc.description.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 beta-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. | - |
dc.description.statementOfResponsibility | restriction | - |
dc.language | English | - |
dc.publisher | Elsevier | - |
dc.relation.isPartOf | BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS | - |
dc.rights | CC BY-NC-ND 2.0 KR | - |
dc.subject.MESH | Amino Acid Sequence | - |
dc.subject.MESH | Anti-Bacterial Agents / pharmacology* | - |
dc.subject.MESH | Bacterial Proteins / chemistry* | - |
dc.subject.MESH | Bacterial Proteins / metabolism* | - |
dc.subject.MESH | Crystallography, X-Ray | - |
dc.subject.MESH | Hydrophobic and Hydrophilic Interactions | - |
dc.subject.MESH | Ligands | - |
dc.subject.MESH | Lipocalins / chemistry | - |
dc.subject.MESH | Models, Molecular | - |
dc.subject.MESH | Polymyxin B / chemistry | - |
dc.subject.MESH | Polymyxin B / metabolism | - |
dc.subject.MESH | Protein Structure, Secondary | - |
dc.subject.MESH | Pseudomonas aeruginosa / metabolism* | - |
dc.subject.MESH | Recombinant Proteins / chemistry | - |
dc.subject.MESH | Recombinant Proteins / metabolism | - |
dc.subject.MESH | Solubility | - |
dc.subject.MESH | Structural Homology, Protein | - |
dc.subject.MESH | Ubiquinone / chemistry | - |
dc.subject.MESH | Ubiquinone / metabolism | - |
dc.title | Crystal structure of the Pseudomonas aeruginosa PA0423 protein and its functional implication in antibiotic sequestration | - |
dc.type | Article | - |
dc.contributor.college | College of Medicine (의과대학) | - |
dc.contributor.department | Dept. of Microbiology (미생물학교실) | - |
dc.contributor.googleauthor | Choongdeok Lee | - |
dc.contributor.googleauthor | Meong Il Kim | - |
dc.contributor.googleauthor | Jaewan Park | - |
dc.contributor.googleauthor | Junghun Kim | - |
dc.contributor.googleauthor | Hansol Oh | - |
dc.contributor.googleauthor | Yoeseph Cho | - |
dc.contributor.googleauthor | Junghyun Son | - |
dc.contributor.googleauthor | Bo-Young Jeon | - |
dc.contributor.googleauthor | Hakhyun Ka | - |
dc.contributor.googleauthor | Minsun Hong | - |
dc.identifier.doi | 10.1016/j.bbrc.2020.05.023 | - |
dc.relation.journalcode | J00281 | - |
dc.identifier.eissn | 1090-2104 | - |
dc.identifier.pmid | 32451086 | - |
dc.identifier.url | https://www.sciencedirect.com/science/article/pii/S0006291X20309293 | - |
dc.citation.volume | 528 | - |
dc.citation.number | 1 | - |
dc.citation.startPage | 85 | - |
dc.citation.endPage | 91 | - |
dc.identifier.bibliographicCitation | BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS, Vol.528(1) : 85-91, 2020-07 | - |
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