ArticlePLoS computational biology2013
Variations within class-A β-lactamase physiochemical properties reflect evolutionary and environmental patterns, but not antibiotic specificity.
Article in PLoS computational biology, 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.
- Exploring complexity of class-A Beta-lactamase family using physiochemical-based multiplex networks.Scientific reports · 2023Article
- Mutation of the conserved Asp-Asp pair impairs the structure, function, and inhibition of CTX-M Class A β-lactamase.FEBS letters · 2021Article
- Toho-1 β-lactamase: backbone chemical shift assignments and changes in dynamics upon binding with avibactam.Journal of biomolecular NMR · 2021Article
- The Class A Carbapenemases BKC-1 and GPC-1 Both Originate from the Bacterial GenusAntimicrobial agents and chemotherapy · 2020Article
- Predicting allostery and microbial drug resistance with molecular simulations.Current opinion in structural biology · 2018Review
- Defining the architecture of KPC-2 Carbapenemase: identifying allosteric networks to fight antibiotics resistance.Scientific reports · 2018Article
- Structure and Functional Characterisation of a Distinctive β-Lactamase from an Environmental Strain EMB20 of Bacillus cereus.Applied biochemistry and biotechnology · 2018Article
- Novel Computational Protocols for Functionally Classifying and Characterising Serine Beta-Lactamases.PLoS computational biology · 2016Article
- Mutations in Antibody Fragments Modulate Allosteric Response Via Hydrogen-Bond Network Fluctuations.Biophysical journal · 2016Article
- Rigidity Emerges during Antibody Evolution in Three Distinct Antibody Systems: Evidence from QSFR Analysis of Fab Fragments.PLoS computational biology · 2015Article
- Ligand-Induced Proton Transfer and Low-Barrier Hydrogen Bond Revealed by X-ray Crystallography.Journal of the American Chemical Society · 2015Article
- Structure-based design of combinatorial mutagenesis libraries.Protein science : a publication of the Protein Society · 2015Article
- Multidrug-resistant phenotype and isolation of a novel SHV- beta-Lactamase variant in a clinical isolate of Enterobacter cloacae.Journal of biomedical science · 2015Article
- Flexibility Correlation between Active Site Regions Is Conserved across Four AmpC β-Lactamase Enzymes.PloS one · 2015Article
- Redistribution of flexibility in stabilizing antibody fragment mutants follows Le Châtelier's principle.PloS one · 2014Article
- A case study comparing quantitative stability-flexibility relationships across five metallo-β-lactamases highlighting differences within NDM-1.Methods in molecular biology (Clifton, N.J.) · 2014Article
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3 authors.
Funding
Abstract
The bacterial enzyme β-lactamase hydrolyzes the β-lactam ring of penicillin and chemically related antibiotics, rendering them ineffective. Due to rampant antibiotic overuse, the enzyme is evolving new resistance activities at an alarming rate. Related, the enzyme's global physiochemical properties exhibit various amounts of conservation and variability across the family. To that end, we characterize the extent of property conservation within twelve different class-A β-lactamases, and conclusively establish that the systematic variations therein parallel their evolutionary history. Large and systematic differences within electrostatic potential maps and pairwise residue-to-residue couplings are observed across the protein, which robustly reflect phylogenetic outgroups. Other properties are more conserved (such as residue pKa values, electrostatic networks, and backbone flexibility), yet they also have systematic variations that parallel the phylogeny in a statistically significant way. Similarly, the above properties also parallel the environmental condition of the bacteria they are from in a statistically significant way. However, it is interesting and surprising that the only one of the global properties (protein charge) parallels the functional specificity patterns; meaning antibiotic resistance activities are not significantly constraining the global physiochemical properties. Rather, extended spectrum activities can emerge from the background of nearly any set of electrostatic and dynamic properties.
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