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• W2097719059 abstract "Class D β-lactamases, a major source of bacterial resistance to β-lactam antibiotic therapies, represent a distinct subset of the β-lactamase superfamily. They share a serine hydrolase mechanism with Classes A/C vs. Class B. Further understanding of their sequence–structure–function relationships would benefit efforts to design a new generation of antibiotics as well as to predict evolutionary mechanisms in response to such therapies. Here we describe analyses based on our high-resolution multiple sequence alignment and phylogenetic tree of ∼80 Class D β-lactamases that leverage several 3D structures of these enzymes. We observe several sequence clusters on the phylogenetic tree, some that are species specific while others include several species from α-, β- and γ-proteobacteria. Residues characteristic of a specific cluster were identified and shown to be located just outside the active site, possibly modulating the function of the catalytic residues to facilitate reactions with specific types of β-lactams. Most significant was the discovery of a likely disulfide bond in a large group composed of α-, β- and γ-proteobacteria that would contribute to enzyme stability and hence bacterial viability under antibiotic assault. A network of co-evolving residues was identified which suggested the importance of maintaining a surface for binding a highly conserved Phe69." @default.
• W2097719059 created "2016-06-24" @default.
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• W2097719059 date "2011-08-22" @default.
• W2097719059 modified "2023-09-27" @default.
• W2097719059 title "The Class D β-lactamase family: residues governing the maintenance and diversity of function" @default.
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• W2097719059 doi "https://doi.org/10.1093/protein/gzr041" @default.
• W2097719059 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/3170078" @default.
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• W2097719059 hasPublicationYear "2011" @default.
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