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• W2058232170 startingPage "1484" @default.
• W2058232170 abstract "β-Lactams are the most commonly prescribed class of antibiotics and have had an enormous impact on human health. Thus, it is disquieting that an enzyme called New Delhi metallo-β-lactamase-1 (NDM-1) can confer Enterobacteriaceae with nearly complete resistance to all β-lactam antibiotics including the carbapenams. We have determined the crystal structure of Klebsiella pneumoniae apo-NDM-1 to 2.1-Å resolution. From the structure, we see that NDM-1 has an expansive active site with a unique electrostatic profile, which we propose leads to a broader substrate specificity. In addition, NDM-1 undergoes important conformational changes upon substrate binding. These changes have not been previously observed in metallo-β-lactamase enzymes and may have a direct influence on substrate recognition and catalysis." @default.
• W2058232170 created "2016-06-24" @default.
• W2058232170 creator A5022292484 @default.
• W2058232170 creator A5056122200 @default.
• W2058232170 date "2011-08-02" @default.
• W2058232170 modified "2023-09-27" @default.
• W2058232170 title "Crystal structure of New Delhi metallo-β-lactamase reveals molecular basis for antibiotic resistance" @default.
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• W2058232170 doi "https://doi.org/10.1002/pro.697" @default.
• W2058232170 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/3190144" @default.
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• W2058232170 hasPublicationYear "2011" @default.
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