Comparison of the Internal Dynamics of Metalloproteases Provides New Insights on Their Function and Evolution.

ABSTRACT: Metalloproteases have evolved in a vast number of biological systems, being one of the most diverse types of proteases and presenting a wide range of folds and catalytic metal ions. Given the increasing understanding of protein internal dynamics and its role in enzyme function, we are interested in assessing how the structural heterogeneity of metalloproteases translates into their dynamics. Therefore, the dynamical profile of the clan MA type protein thermolysin, derived from an Elastic Network Model of protein structure, was evaluated against those obtained from a set of experimental structures and molecular dynamics simulation trajectories. A close correspondence was obtained between modes derived from the coarse-grained model and the subspace of functionally-relevant motions observed e

SUBMITTER: Carvalho HF 

PROVIDER: S-EPMC4580569 | biostudies-literature | 2015

REPOSITORIES: biostudies-literature