TY  - JOUR
AU  - Arinkin, Vladimir
AU  - Granzin, Joachim
AU  - Röllen, Katrin
AU  - Krauss, Ulrich
AU  - Jaeger, Karl-Erich
AU  - Willbold, Dieter
AU  - Batra-Safferling, Renu
TI  - Structure of a LOV protein in apo-state and implications for construction of LOV-based optical tools
JO  - Scientific reports
VL  - 7
SN  - 2045-2322
CY  - London
PB  - Nature Publishing Group
M1  - FZJ-2018-00524
SP  - 42971 -
PY  - 2017
AB  - 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.
LB  - PUB:(DE-HGF)16
C6  - pmid:28211532
UR  - <Go to ISI:>//WOS:000394486200001
DO  - DOI:10.1038/srep42971
UR  - https://juser.fz-juelich.de/record/842277
ER  -