From crystallographic data to the solution structure of photoreceptors: the case of the AppA BLUF domain.

ABSTRACT: Photoreceptor proteins bind a chromophore, which, upon light absorption, modifies its geometry or its interactions with the protein, finally inducing the structural change needed to switch the protein from an inactive to an active or signaling state. In the Blue Light-Using Flavin (BLUF) family of photoreceptors, the chromophore is a flavin and the changes have been connected with a rearrangement of the hydrogen bond network around it on the basis of spectroscopic changes measured for the dark-to-light conversion. However, the exact conformational change triggered by the photoexcitation is still elusive mainly because a clear consensus on the identity not only of the light activated state but also of the dark one has not been achieved. Here, we present an integrated investigation that comb

SUBMITTER: Hashem S 

PROVIDER: S-EPMC8528011 | biostudies-literature | 2021 Oct

REPOSITORIES: biostudies-literature