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

doi:10.1016/0167-4838(94)00187-l

Back to search

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 residu...

Topics

Anti-Bacterial Agents
Base Sequence
Binding Sites
Escherichia coli
Kinetics
Molecular Sequence Data
Molecular Structure
Mutagenesis, Site-Directed
Phenotype
Plasmids
beta-Lactamases
beta-Lactams

Community interpretation

Discuss the evidence

Ask a question, add context or challenge an interpretation. Community activity is separate from scientific evidence strength.

discussions

replies

Citations encouraged

Claims remain attributable.

No discussion yet

Be the first to add a careful, cited interpretation.