Systematic substitutions at BLIP position 50 result in changes in binding specificity for class A β-lactamases.

ABSTRACT:

Background

The production of β-lactamases by bacteria is the most common mechanism of resistance to the widely prescribed β-lactam antibiotics. β-lactamase inhibitory protein (BLIP) competitively inhibits class A β-lactamases via two binding loops that occlude the active site. It has been shown that BLIP Tyr50 is a specificity determinant in that substitutions at this position result in large differential changes in the relative affinity of BLIP for class A β-lactamases.

Results

In this study, the effect of systematic substitutions at BLIP position 50 on binding to class A β-lactamases was examined to further explore the role of BLIP Tyr50 in modulating specificity. The results indicate the sequence requirements at position 50 are widely different depending on the target β-l

SUBMITTER: Adamski CJ 

PROVIDER: S-EPMC5340008 | biostudies-literature | 2017 Mar

REPOSITORIES: biostudies-literature