ArticleThe Biochemical journal2013
Solution structures of the Bacillus cereus metallo-β-lactamase BcII and its complex with the broad spectrum inhibitor R-thiomandelic acid.
Article in The Biochemical journal, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.
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Who cites it
16 citing papers in PubMed, 32 citations in OpenAlex.
- Restoring Meropenem Activity Against VIM-1-Producing Klebsiella pneumoniae Through Zinc-Binding Ligands.Chembiochem : a European journal of chemical biology · 2026Article
- Revisiting the Metallo-International journal of microbiology · 2025Review
- Comparative Analysis of Bacillus cereus Group Isolates' Resistance Using Disk Diffusion and Broth Microdilution and the Correlation between Antimicrobial Resistance Phenotypes and Genotypes.Applied and environmental microbiology · 2022Article
- Metallo-β-lactamases in the Age of Multidrug Resistance: From Structure and Mechanism to Evolution, Dissemination, and Inhibitor Design.Chemical reviews · 2021Review
- Structural Insights for Core Scaffold and Substrate Specificity of B1, B2, and B3 Metallo-β-Lactamases.Frontiers in microbiology · 2021Article
- Article
- The Continuing Challenge of Metallo-β-Lactamase Inhibition: Mechanism Matters.Trends in pharmacological sciences · 2018Review
- Thiol-Containing Metallo-β-Lactamase Inhibitors Resensitize Resistant Gram-Negative Bacteria to Meropenem.ACS infectious diseases · 2017Article
- Crystallographic analyses of isoquinoline complexes reveal a new mode of metallo-β-lactamase inhibition.Chemical communications (Cambridge, England) · 2017Article
- Cyclic Boronates Inhibit All Classes of β-Lactamases.Antimicrobial agents and chemotherapy · 2017Article
- Use of ferrous iron by metallo-β-lactamases.Journal of inorganic biochemistry · 2016Article
- The Role of Active Site Flexible Loops in Catalysis and of Zinc in Conformational Stability of Bacillus cereus 569/H/9 β-Lactamase.The Journal of biological chemistry · 2016Article
- Overcoming differences: The catalytic mechanism of metallo-β-lactamases.FEBS letters · 2015Review
- Crystal Structure of DIM-1, an Acquired Subclass B1 Metallo-β-Lactamase from Pseudomonas stutzeri.PloS one · 2015Article
- Rhodanine hydrolysis leads to potent thioenolate mediated metallo-β-lactamase inhibition.Nature chemistry · 2014Article
- Evolution of Metallo-β-lactamases: Trends Revealed by Natural Diversity and in vitro Evolution.Antibiotics (Basel, Switzerland) · 2014Article
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3 authors at 1 institution in 1 country.
Funding
Abstract
Metallo-β-lactamases, enzymes which inactivate β-lactam antibiotics, are of increasing biological and clinical significance as a source of antibiotic resistance in pathogenic bacteria. In the present study we describe the high-resolution solution NMR structures of the Bacillus cereus metallo-β-lactamase BcII and of its complex with R-thiomandelic acid, a broad-spectrum inhibitor of metallo-β-lactamases. This is the first reported solution structure of any metallo-β-lactamase. There are differences between the solution structure of the free enzyme and previously reported crystal structures in the loops flanking the active site, which are important for substrate and inhibitor binding and catalysis. The binding of R-thiomandelic acid and the roles of active-site residues are defined in detail. Changes in the enzyme structure upon inhibitor binding clarify the role of the mobile β3-β4 loop. Comparisons with other metallo-β-lactamases highlight the roles of individual amino-acid residues in the active site and the β3-β4 loop in inhibitor binding and provide information on the basis of structure-activity relationships among metallo-β-lactamase inhibitors.
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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.