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000842277 1001_ $$0P:(DE-Juel1)161543$$aArinkin, Vladimir$$b0
000842277 245__ $$aStructure of a LOV protein in apo-state and implications for construction of LOV-based optical tools
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000842277 520__ $$aUnique features of Light-Oxygen-Voltage (LOV) proteins like relatively small size (~12–19 kDa), inherent modularity, highly-tunable photocycle and oxygen-independent fluorescence have lately been exploited for the generation of optical tools. Structures of LOV domains reported so far contain a flavin chromophore per protein molecule. Here we report two new findings on the short LOV protein W619_1-LOV from Pseudomonas putida. First, the apo-state crystal structure of W619_1-LOV at 2.5 Å resolution reveals conformational rearrangements in the secondary structure elements lining the chromophore pocket including elongation of the Fα helix, shortening of the Eα-Fα loop and partial unfolding of the Eα helix. Second, the apo W619_1-LOV protein binds both natural and structurally modified flavin chromophores. Remarkably different photophysical and photochemical properties of W619_1-LOV bound to 7-methyl-8-chloro-riboflavin (8-Cl-RF) and lumichrome imply application of these variants as novel optical tools as they offer advantages such as no adduct state formation, and a broader choice of wavelengths for in vitro studies.
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000842277 7001_ $$0P:(DE-Juel1)131965$$aGranzin, Joachim$$b1
000842277 7001_ $$0P:(DE-Juel1)157880$$aRöllen, Katrin$$b2
000842277 7001_ $$0P:(DE-Juel1)131482$$aKrauss, Ulrich$$b3
000842277 7001_ $$0P:(DE-Juel1)131457$$aJaeger, Karl-Erich$$b4
000842277 7001_ $$0P:(DE-Juel1)132029$$aWillbold, Dieter$$b5
000842277 7001_ $$0P:(DE-Juel1)131950$$aBatra-Safferling, Renu$$b6$$eCorresponding author
000842277 773__ $$0PERI:(DE-600)2615211-3$$a10.1038/srep42971$$gVol. 7, p. 42971 -$$p42971 -$$tScientific reports$$v7$$x2045-2322$$y2017
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