ArticleAntimicrobial agents and chemotherapy2014
Crystal structure of carbapenemase OXA-58 from Acinetobacter baumannii.
Article in Antimicrobial agents and chemotherapy, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 27 papers, 1 of them a synthesis that pooled it.
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Who cites it
27 citing papers in PubMed, 1 synthesis or guideline pooled it, 37 citations in OpenAlex.
- Structural basis for carbapenem-hydrolyzing mechanisms of carbapenemases conferring antibiotic resistance.International journal of molecular sciences · 2015Pooled it
- An Integrated Computational and Biophysical Approach for Investigating the Structure-Function Impact of blaOXA-58 Mutations in Acinetobacter baumannii.Molecular biotechnology · 2026Article
- Structural insights into the activity of carbapenemases: understanding the mechanism of action of current inhibitors and informing the design of new carbapenem adjuvants.RSC medicinal chemistry · 2025Review
- The lipoprotein biosynthesis pathway: key to OXA-mediated carbapenem resistance inAntimicrobial agents and chemotherapy · 2025Article
- Structural comparison of substrate-binding pockets of serine β-lactamases in classes A, C, and D.Journal of enzyme inhibition and medicinal chemistry · 2025Review
- Standardized Residue Numbering and Secondary Structure Nomenclature in the Class D β-Lactamases.ACS infectious diseases · 2025Article
- Standardized Residue Numbering and Secondary Structure Nomenclature in the Class D β-Lactamases.bioRxiv : the preprint server for biology · 2025Article
- Decarboxylation of the Catalytic Lysine Residue by the C5α-Methyl-Substituted Carbapenem NA-1-157 Leads to Potent Inhibition of the OXA-58 Carbapenemase.ACS infectious diseases · 2024Article
- Structural and Dynamic Features of Acinetobacter baumannii OXA-66 β-Lactamase Explain Its Stability and Evolution of Novel Variants.Journal of molecular biology · 2024Article
- The Dynamics of OXA-23 β-Lactamase fromInternational journal of molecular sciences · 2023Article
- OXA-48-Like β-Lactamases: Global Epidemiology, Treatment Options, and Development Pipeline.Antimicrobial agents and chemotherapy · 2022Review
- Structural and Functional Characterization of OXA-48: Insight into Mechanism and Structural Basis of Substrate Recognition and Specificity.International journal of molecular sciences · 2021Article
- Inhibition of theACS infectious diseases · 2021Article
- A surface loop modulates activity of the Bacillus class D β-lactamases.Journal of structural biology · 2020Article
- Molecular Mechanisms, Epidemiology, and Clinical Importance of β-Lactam Resistance inInternational journal of molecular sciences · 2020Review
- Structure-Based Screening of Non-β-Lactam Inhibitors against Class D β-Lactamases: An Approach of Docking and Molecular Dynamics.ACS omega · 2020Article
- The crystal structures of CDD-1, the intrinsic class D β-lactamase from the pathogenic Gram-positive bacterium Clostridioides difficile, and its complex with cefotaxime.Journal of structural biology · 2019Article
- β-Lactamases and β-Lactamase Inhibitors in the 21st Century.Journal of molecular biology · 2019Review
- Exploring the potential of boronic acids as inhibitors of OXA-24/40 β-lactamase.Protein science : a publication of the Protein Society · 2017Article
- Clinical Variants of the Native Class D β-Lactamase of Acinetobacter baumannii Pose an Emerging Threat through Increased Hydrolytic Activity against Carbapenems.Antimicrobial agents and chemotherapy · 2016Article
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Authors and funding
4 authors at 2 institutions in 1 country.
Funding
Abstract
Class D β-lactamases capable of hydrolyzing last-resort carbapenem antibiotics represent a major challenge for treatment of bacterial infections. Wide dissemination of these enzymes in Acinetobacter baumannii elevated this pathogen to the category of most deadly and difficult to treat. We present here the structure of the OXA-58 β-lactamase, a major class D carbapenemase of A. baumannii, determined to 1.30-Å resolution. Unlike two other Acinetobacter carbapenemases, OXA23 and OXA-24, the OXA-58 enzyme lacks the characteristic hydrophobic bridge over the active site, despite conservation of the residues which participate in its formation. The active-site residues in OXA-58 are spatially conserved in comparison to those in other class D β-lactamases. Lys86, which activates water molecules during the acylation and deacylation steps, is fully carboxylated in the OXA-58 structure. In the absence of a substrate, a water molecule is observed in the active site of the enzyme and is positioned in the pocket that is usually occupied by the 6α-hydroxyethyl moiety of carbapenems. A water molecule in this location would efficiently deacylate good substrates, such as the penicillins, but in the case of carbapenems, it would be expelled by the 6α-hydroxyethyl moiety of the antibiotics and a water from the surrounding medium would find its way to the vicinity of the carboxylated Lys86 to perform deacylation. Subtle differences in the position of this water in the acyl-enzyme complexes of class D β-lactamases could ultimately be responsible for differences in the catalytic efficiencies of these enzymes against last-resort carbapenem antibiotics.
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