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Article

Complementary roles of mutations at positions 69 and 242 in a class A beta-lactamase.

Biochimica et biophysica acta - 22 Feb 1995

Bonomo R A, Dawes C G, Knox J R, Shlaes D M

Abstract excerpt

Analysis of the three-dimensional structure of class A beta-lactamases suggests that deformation of the substrate binding site can be produced by changes in the hydrophobicity of residue 69 behind the beta-sheet and by outward movement of the B3 beta-strand by introduction of a non-glycine residue at position 242 on the B4 beta-strand. By site-directed mutagenesis Met69-IleGly242-Cys, a double mutant, of the...

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PMID: 7873579
DOI: 10.1016/0167-4838(94)00187-l

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-08.1.

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