ArticleAntimicrobial agents and chemotherapy2010
Crystal structure of the narrow-spectrum OXA-46 class D beta-lactamase: relationship between active-site lysine carbamylation and inhibition by polycarboxylates.
Article in Antimicrobial agents and chemotherapy, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 24 papers.
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Who cites it
24 citing papers in PubMed.
- Structural comparison of substrate-binding pockets of serine β-lactamases in classes A, C, and D.Journal of enzyme inhibition and medicinal chemistry · 2025Review
- Diversity in the Common Fold: Structural Insights into Class D β-Lactamases from Gram-Negative Pathogens.Pathogens (Basel, Switzerland) · 2025Article
- Activity of the β-Lactamase Inhibitor LN-1-255 against Carbapenem-Hydrolyzing Class D β-Lactamases from Acinetobacter baumannii.Antimicrobial agents and chemotherapy · 2017Article
- Crystal Structure of the Pseudomonas aeruginosa BEL-1 Extended-Spectrum β-Lactamase and Its Complexes with Moxalactam and Imipenem.Antimicrobial agents and chemotherapy · 2016Article
- In vivo protein interaction network analysis reveals porin-localized antibiotic inactivation in Acinetobacter baumannii strain AB5075.Nature communications · 2016Article
- 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
- Class D β-lactamases do exist in Gram-positive bacteria.Nature chemical biology · 2016Article
- Purification and characterization of a new β-lactamase OXA-205 from Pseudomonas aeruginosa.Annals of clinical microbiology and antimicrobials · 2015Article
- Structural Basis for Enhancement of Carbapenemase Activity in the OXA-51 Family of Class D β-Lactamases.ACS chemical biology · 2015Article
- Structural Basis for Different Substrate Profiles of Two Closely Related Class D β-Lactamases and Their Inhibition by Halogens.Biochemistry · 2015Article
- Article
- Acquired Class D β-Lactamases.Antibiotics (Basel, Switzerland) · 2014Review
- Fragment-based inhibitor discovery against β-lactamase.Future medicinal chemistry · 2014Review
- Crystal structure of carbapenemase OXA-58 from Acinetobacter baumannii.Antimicrobial agents and chemotherapy · 2014Article
- Structural origins of oxacillinase specificity in class D β-lactamases.Antimicrobial agents and chemotherapy · 2014Article
- Class D β-lactamases: a reappraisal after five decades.Accounts of chemical research · 2013Review
- Structures of the class D Carbapenemases OXA-23 and OXA-146: mechanistic basis of activity against carbapenems, extended-spectrum cephalosporins, and aztreonam.Antimicrobial agents and chemotherapy · 2013Article
- Structural basis for carbapenemase activity of the OXA-23 β-lactamase from Acinetobacter baumannii.Chemistry & biology · 2013Article
- Crystal structures of bifunctional penicillin-binding protein 4 from Listeria monocytogenes.Antimicrobial agents and chemotherapy · 2013Article
- Bacterial cell-wall recycling.Annals of the New York Academy of Sciences · 2013Review
Corrections and comments
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8 authors.
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Abstract
Class D beta-lactamases represent a heterogeneous group of active-site serine beta-lactamases that show an extraordinary panel of functional features and substrate profiles, thus representing relevant models for biochemical and structural studies. OXA-46 is a narrow-spectrum enzyme belonging to the OXA-2 subgroup which was found in a Pseudomonas aeruginosa clinical isolate from northern Italy. In this work, we obtained the three-dimensional structure of OXA-46, which shows the overall fold of active serine beta-lactamases and a dimeric quaternary structure. Significant differences with currently available structures of class D beta-lactamases were found in the loops located close to the active site, which differ in length and conformation. Interestingly, the three subunits present in the asymmetric unit showed some structural heterogeneity, only one of which presented a carbamylated lysine recognized as an important functional feature of class D enzymes. The carbamylation state of residue Lys75 appeared to be associated with different shapes and dimensions of the active site. Moreover, a tartrate molecule from the crystallization buffer was found in the active site of the noncarbamylated subunits, which interacts with catalytically relevant residues. The OXA-46 crystal asymmetric units thus interestingly present the structures of the free carbamylated active site and of the ligand-bound uncarbamylated active site, offering the structural basis for investigating the potential of new scaffolds of beta-lactamase inhibitors.
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