Structural dynamics in the evolution of a bilobed protein scaffold.

ABSTRACT: Novel biophysical tools allow the structural dynamics of proteins and the regulation of such dynamics by binding partners to be explored in unprecedented detail. Although this has provided critical insights into protein function, the means by which structural dynamics direct protein evolution remain poorly understood. Here, we investigated how proteins with a bilobed structure, composed of two related domains from the periplasmic-binding protein-like II domain family, have undergone divergent evolution, leading to adaptation of their structural dynamics. We performed a structural analysis on ∼600 bilobed proteins with a common primordial structural core, which we complemented with biophysical studies to explore the structural dynamics of selected examples by single-molecule Förster resonan

SUBMITTER: Gouridis G 

PROVIDER: S-EPMC8694067 | biostudies-literature | 2021 Dec

REPOSITORIES: biostudies-literature