Binding of cephalothin and cefotaxime to D-Ala-D-Ala-peptidase reveals a functional basis of a natural mutation in a low-affinity penicillin-binding protein and in extended-spectrum .beta.-lactamases

doi:10.1021/bi00029a030

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Article

Binding of cephalothin and cefotaxime to D-Ala-D-Ala-peptidase reveals a functional basis of a natural mutation in a low-affinity penicillin-binding protein and in extended-spectrum .beta.-lactamases

25 Jul 1995

Abstract excerpt

Two clinically-important beta-lactam antibiotics, cephalothin and cefotaxime, have been observed by X-ray crystallography bound to the reactive Ser62 of the D-alanyl-D-alanine carboxypeptidase/transpeptidase of Streptomyces sp. R61. Refinement of the two crystal structures produced R factors for 3 sigma (F) data of 0.166 (to 1.8 A) and 0.170 (to 2.0 A) for the cephalothin and cefotaxime complexes, respectively....

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PMID: 7626623
DOI: 10.1021/bi00029a030

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