ArticleThe Journal of biological chemistry2014
Crystal structure of the dithiol oxidase DsbA enzyme from proteus mirabilis bound non-covalently to an active site peptide ligand.
Article in The Journal of biological chemistry, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.
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Who cites it
12 citing papers in PubMed.
- Structural and functional specialization of Bordetella pertussis DsbA for pertussis toxin folding.Protein science : a publication of the Protein Society · 2026Article
- Exploring the inhibitory potential ofFrontiers in molecular biosciences · 2023Article
- Interplay between DsbA1, DsbA2 and C8J_1298 Periplasmic Oxidoreductases ofInternational journal of molecular sciences · 2021Article
- DsbA is a redox-switchable mechanical chaperone.Chemical science · 2021Article
- Structural bioinformatic analysis of DsbA proteins and their pathogenicity associated substrates.Computational and structural biotechnology journal · 2021Review
- Disulfide Bond Formation in the Periplasm ofEcoSal Plus · 2019Review
- Approaches to the Structure-Based Design of Antivirulence Drugs: Therapeutics for the Post-Antibiotic Era.Molecules (Basel, Switzerland) · 2019Review
- Inhibition of Diverse DsbA Enzymes in Multi-DsbA Encoding Pathogens.Antioxidants & redox signaling · 2018Article
- Bacterial thiol oxidoreductases - from basic research to new antibacterial strategies.Applied microbiology and biotechnology · 2017Review
- Targeting Bacterial Dsb Proteins for the Development of Anti-Virulence Agents.Molecules (Basel, Switzerland) · 2016Review
- Monitoring Oxidative Folding of a Single Protein Catalyzed by the Disulfide Oxidoreductase DsbA.The Journal of biological chemistry · 2015Article
- Virtual Screening of Peptide and Peptidomimetic Fragments Targeted to Inhibit Bacterial Dithiol Oxidase DsbA.PloS one · 2015Article
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Authors and funding
6 authors.
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Abstract
The disulfide bond forming DsbA enzymes and their DsbB interaction partners are attractive targets for development of antivirulence drugs because both are essential for virulence factor assembly in Gram-negative pathogens. Here we characterize PmDsbA from Proteus mirabilis, a bacterial pathogen increasingly associated with multidrug resistance. PmDsbA exhibits the characteristic properties of a DsbA, including an oxidizing potential, destabilizing disulfide, acidic active site cysteine, and dithiol oxidase catalytic activity. We evaluated a peptide, PWATCDS, derived from the partner protein DsbB and showed by thermal shift and isothermal titration calorimetry that it binds to PmDsbA. The crystal structures of PmDsbA, and the active site variant PmDsbAC30S were determined to high resolution. Analysis of these structures allows categorization of PmDsbA into the DsbA class exemplified by the archetypal Escherichia coli DsbA enzyme. We also present a crystal structure of PmDsbAC30S in complex with the peptide PWATCDS. The structure shows that the peptide binds non-covalently to the active site CXXC motif, the cis-Pro loop, and the hydrophobic groove adjacent to the active site of the enzyme. This high-resolution structural data provides a critical advance for future structure-based design of non-covalent peptidomimetic inhibitors. Such inhibitors would represent an entirely new antibacterial class that work by switching off the DSB virulence assembly machinery.
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