Structure and function of a short LOV protein from the marine phototrophic bacterium Dinoroseobacter shibae.

ABSTRACT:

Background

Light, oxygen, voltage (LOV) domains are widely distributed in plants, algae, fungi, bacteria, and represent the photo-responsive domains of various blue-light photoreceptor proteins. Their photocycle involves the blue-light triggered adduct formation between the C(4a) atom of a non-covalently bound flavin chromophore and the sulfur atom of a conserved cysteine in the LOV sensor domain. LOV proteins show considerable variation in the structure of N- and C-terminal elements which flank the LOV core domain, as well as in the lifetime of the adduct state.

Results

Here, we report the photochemical, structural and functional characterization of DsLOV, a LOV protein from the photoheterotrophic marine α-proteobacterium Dinoroseobacter shibae which exhibits an average add

SUBMITTER: Endres S 

PROVIDER: S-EPMC4335406 | biostudies-literature | 2015 Feb

REPOSITORIES: biostudies-literature