A case study comparing quantitative stability-flexibility relationships across five metallo-β-lactamases highlighting differences within NDM-1.

ABSTRACT: The Distance Constraint Model (DCM) is an ensemble-based biophysical model that integrates thermodynamic and mechanical viewpoints of protein structure. The DCM outputs a large number of structural characterizations that collectively allow for Quantified Stability-Flexibility Relationships (QSFR) to be identified and compared across protein families. Using five metallo-β-lactamases (MBLs) as a representative set, we demonstrate how QSFR properties are both conserved and varied across protein families. Similar to our characterizations on other protein families, the backbone flexibility of the five MBLs are overall visually conserved, yet there are interesting specific quantitative differences. For example, the plasmid-encoded NDM-1 enzyme, which leads to a fast spreading drug-resistant vers

SUBMITTER: Brown MC 

PROVIDER: S-EPMC4676803 | biostudies-literature | 2014

REPOSITORIES: biostudies-literature