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| Hauptseite > Workflowsammlungen > Publikationsgebühren > Structure of a LOV protein in apo-state and implications for construction of LOV-based optical tools |
| Hauptseite > Workflowsammlungen > Publikationsgebühren > Structure of a LOV protein in apo-state and implications for construction of LOV-based optical tools |
| Journal Article | FZJ-2018-00524 |
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2017
Nature Publishing Group
London
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Please use a persistent id in citations: http://hdl.handle.net/2128/16635 doi:10.1038/srep42971
Abstract: 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.
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