Abstract
βLactam antibiotics—the penicillins, cephalosporins and related compounds—act by inhibiting enzymes that catalyse the final stages of the synthesis of bacterial cell walls1,2. Recent crystallo-graphic studies o( representative enzymes3,4 are beginning to reveal the structural bases of antibiotic specificity and mechanism of action, while intensive efforts are being made to understand the βlactamase enzymes that are largely responsible for bacterial resistance to these antibiotics5–8. It has been suggested that the β-lactamases and β-lactam target enzymes may be evolutionary related9 and some similarity of amino-acid sequence around a common active-site serine residue supports this idea10. We present here the first evidence from a comparison of three-dimensional structures in support of this hypothesis: the structure of βlactamase I from Bacillus cereus11 is similar to that of the penicillin-sensitive D-alanyl-D-alanine carboxypeptidase-transpeptidase from Streptomyces R613.
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Samraoui, B., Sutton, B., Todd, R. et al. Tertiary structural similarity between a class A β-lactamase and a penicillin-sensitive D-alanyl carboxypeptidase-transpeptidase. Nature 320, 378–380 (1986). https://doi.org/10.1038/320378a0
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DOI: https://doi.org/10.1038/320378a0
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