A hinge migration mechanism unlocks the evolution of green-to-red photoconversion in GFP-like proteins.

ABSTRACT: In proteins, functional divergence involves mutations that modify structure and dynamics. Here we provide experimental evidence for an evolutionary mechanism driven solely by long-range dynamic motions without significant backbone adjustments, catalytic group rearrangements, or changes in subunit assembly. Crystallographic structures were determined for several reconstructed ancestral proteins belonging to a GFP class frequently employed in superresolution microscopy. Their chain flexibility was analyzed using molecular dynamics and perturbation response scanning. The green-to-red photoconvertible phenotype appears to have arisen from a common green ancestor by migration of a knob-like anchoring region away from the active site diagonally across the β barrel fold. The allosterically couple

SUBMITTER: Kim H 

PROVIDER: S-EPMC4370283 | biostudies-literature | 2015 Jan

REPOSITORIES: biostudies-literature