The structural changes in the signaling mechanism of bacteriophytochromes in solution revealed by a multiscale computational investigation.

ABSTRACT: Phytochromes are red-light sensing proteins, with important light-regulatory roles in different organisms, which are capturing an increasing interest in bioimaging and optogenetics. Upon absorption of light by the embedded bilin chromophore, they undergo structural changes that extend from the chromophore to the protein and finally drive the biological function. Up to now, the underlying mechanism still has to be characterized fully. Here we investigate the Pfr activated form of a bacterial phytochrome, by combining extensive molecular dynamics simulations with a polarizable QM/MM description of the spectroscopic properties, revealing a large structure relaxation in solution, compared to the crystal structure, both in the chromophore-binding pocket and in the overall structure of the phyto

SUBMITTER: Macaluso V 

PROVIDER: S-EPMC8179611 | biostudies-literature | 2021 Mar

REPOSITORIES: biostudies-literature