ArticleAntimicrobial agents and chemotherapy2013
Structural analysis of the role of Pseudomonas aeruginosa penicillin-binding protein 5 in β-lactam resistance.
Article in Antimicrobial agents and chemotherapy, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 30 papers.
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Who cites it
30 citing papers in PubMed, 46 citations in OpenAlex.
- Molecular Insights into the β‑Lactam α‑Methyl Modulation ofACS omega · 2026Article
- Lytic transglycosylase Slt of Pseudomonas aeruginosa as a periplasmic hub protein.Protein science : a publication of the Protein Society · 2024Article
- Penicillin-binding protein redundancy inApplied and environmental microbiology · 2024Article
- Drug Discovery in the Field of β-Lactams: An Academic Perspective.Antibiotics (Basel, Switzerland) · 2024Review
- Resistance inAntibiotics (Basel, Switzerland) · 2023Review
- Amber-codon suppression for spatial localization and in vivo photoaffinity capture of the interactome of the Pseudomonas aeruginosa rare lipoprotein A lytic transglycosylase.Protein science : a publication of the Protein Society · 2023Article
- Penicillin-Binding Protein 5/6 Acting as a Decoy Target in Pseudomonas aeruginosa Identified by Whole-Cell Receptor Binding and Quantitative Systems Pharmacology.Antimicrobial agents and chemotherapy · 2023Article
- PBP Target Profiling by β-Lactam and β-Lactamase Inhibitors in Intact Pseudomonas aeruginosa: Effects of the Intrinsic and Acquired Resistance Determinants on the Periplasmic Drug Availability.Microbiology spectrum · 2023Article
- Comparative Modeling and Analysis of Extremophilic D-Ala-D-Ala Carboxypeptidases.Biomolecules · 2023Article
- Vancomycin Resistance inMicroorganisms · 2022Review
- Structural Insights into Substrate Binding and Antibiotic Inhibition of Enterobacterial Penicillin-Binding Protein 6.Life (Basel, Switzerland) · 2022Article
- β-Lactam antibiotic targets and resistance mechanisms: from covalent inhibitors to substrates.RSC medicinal chemistry · 2021Review
- Brief survey on organometalated antibacterial drugs and metal-based materials with antibacterial activity.RSC chemical biology · 2021Review
- Phenotypic and genomic characterization ofCurrent research in food science · 2021Article
- Molecular mechanisms of vancomycin resistance.Protein science : a publication of the Protein Society · 2020Review
- Influence of the α-Methoxy Group on the Reaction of Temocillin with Pseudomonas aeruginosa PBP3 and CTX-M-14 β-Lactamase.Antimicrobial agents and chemotherapy · 2019Article
- The Role of the Ω-Loop in Regulation of the Catalytic Activity of TEM-Type β-Lactamases.Biomolecules · 2019Review
- Past and Present Perspectives on β-Lactamases.Antimicrobial agents and chemotherapy · 2018Review
- Article
- Substitution of Alanine at Position 184 with Glutamic Acid in Escherichia coli PBP5 Ω-Like Loop Introduces a Moderate Cephalosporinase Activity.The protein journal · 2018Article
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Authors and funding
10 authors at 2 institutions in 1 country.
Funding
Abstract
Penicillin-binding protein 5 (PBP5) is one of the most abundant PBPs in Pseudomonas aeruginosa. Although its main function is that of a cell wall dd-carboxypeptidase, it possesses sufficient β-lactamase activity to contribute to the ability of P. aeruginosa to resist the antibiotic activity of the β-lactams. The study of these dual activities is important for understanding the mechanisms of antibiotic resistance by P. aeruginosa, an important human pathogen, and to the understanding of the evolution of β-lactamase activity from the PBP enzymes. We purified a soluble version of P. aeruginosa PBP5 (designated Pa sPBP5) by deletion of its C-terminal membrane anchor. Under in vitro conditions, Pa sPBP5 demonstrates both dd-carboxypeptidase and expanded-spectrum β-lactamase activities. Its crystal structure at a 2.05-Å resolution shows features closely resembling those of the class A β-lactamases, including a shortened loop spanning residues 74 to 78 near the active site and with respect to the conformations adopted by two active-site residues, Ser101 and Lys203. These features are absent in the related PBP5 of Escherichia coli. A comparison of the two Pa sPBP5 monomers in the asymmetric unit, together with molecular dynamics simulations, revealed an active-site flexibility that may explain its carbapenemase activity, a function that is absent in the E. coli PBP5 enzyme. Our functional and structural characterizations underscore the versatility of this PBP5 in contributing to the β-lactam resistance of P. aeruginosa while highlighting how broader β-lactamase activity may be encoded in the structural folds shared by the PBP and serine β-lactamase classes.
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