%0 Journal Article
%A Arinkin, Vladimir
%A Granzin, Joachim
%A Röllen, Katrin
%A Krauss, Ulrich
%A Jaeger, Karl-Erich
%A Willbold, Dieter
%A Batra-Safferling, Renu
%T Structure of a LOV protein in apo-state and implications for construction of LOV-based optical tools
%J Scientific reports
%V 7
%@ 2045-2322
%C London
%I Nature Publishing Group
%M FZJ-2018-00524
%P 42971 -
%D 2017
%X Unique features of Light-Oxygen-Voltage (LOV) proteins like relatively small size (~12–19 kDa), inherent modularity, highly-tunable photocycle and oxygen-independent fluorescence have lately been exploited for the generation of optical tools. Structures of LOV domains reported so far contain a flavin chromophore per protein molecule. Here we report two new findings on the short LOV protein W619_1-LOV from Pseudomonas putida. First, the apo-state crystal structure of W619_1-LOV at 2.5 Å resolution reveals conformational rearrangements in the secondary structure elements lining the chromophore pocket including elongation of the Fα helix, shortening of the Eα-Fα loop and partial unfolding of the Eα helix. Second, the apo W619_1-LOV protein binds both natural and structurally modified flavin chromophores. Remarkably different photophysical and photochemical properties of W619_1-LOV bound to 7-methyl-8-chloro-riboflavin (8-Cl-RF) and lumichrome imply application of these variants as novel optical tools as they offer advantages such as no adduct state formation, and a broader choice of wavelengths for in vitro studies.
%F PUB:(DE-HGF)16
%9 Journal Article
%$ pmid:28211532
%U <Go to ISI:>//WOS:000394486200001
%R 10.1038/srep42971
%U https://juser.fz-juelich.de/record/842277