Illuminating solution responses of a LOV domain protein with photocoupled small-angle X-ray scattering.

ABSTRACT: The PAS-LOV domain is a signal-transducing component found in a large variety of proteins that is responsible for sensing different stimuli such as light, oxygen, and voltage. The LOV protein VVD regulates blue light responses in the filamentous fungi Neurospora crassa. Using photocoupled, time-resolved small-angle X-ray scattering, we extract the solution protein structure in both dark-adapted and light-activated states. Two distinct dark-adapted conformations are detected in the wild-type protein: a compact structure that corresponds to the crystal structure of the dark-state monomer as well as an extended structure that is well modeled by introducing conformational disorder at the N-terminus of the protein. These conformations are accentuated in carefully selected variants, in which a k

SUBMITTER: Lamb JS 

PROVIDER: S-EPMC2858630 | biostudies-literature | 2009 Nov

REPOSITORIES: biostudies-literature