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Time-Resolved X-Ray Solution Scattering Reveals the Structural Photoactivation of a Light-Oxygen-Voltage Photoreceptor

Journal article
Authors Oskar Berntsson
R. P. Diensthuber
Matthijs R. Penman
Alexander Björling
Ashley J Hughes
Léocadie Henry
Stephan Niebling
G. Newby
M. Liebi
A. Menzel
R. Henning
I. Kosheleva
A. Moglich
Sebastian Westenhoff
Published in Structure
Volume 25
Issue 6
Pages 933-938.e3
ISSN 0969-2126
Publication year 2017
Published at Department of Chemistry and Molecular Biology
Pages 933-938.e3
Language en
Keywords biological macromolecules, bacillus-subtilis, lov2 domains, phototropin, protein, ytva, receptor, flavoprotein, transduction, photocycle
Subject categories Biochemistry and Molecular Biology, Cell Biology


Light-oxygen-voltage (LOV) receptors are sensory proteins controlling a wide range of organismal adaptations in multiple kingdoms of life. Because of their modular nature, LOV domains are also attractive for use as optogenetic actuators. A flavin chromophore absorbs blue light, forms a bond with a proximal cysteine residue, and induces changes in the surroundings. There is a gap of knowledge on how this initial signal is relayed further through the sensor to the effector module. To characterize these conformational changes, we apply time-resolved X-ray scattering to the homodimeric LOV domain from Bacillus subtilis YtvA. We observe a global structural change in the LOV dimer synchronous with the formation of the chromophore photoproduct state. Using molecular modeling, this change is identified as splaying apart and relative rotation of the two monomers, which leads to an increased separation at the anchoring site of the effector modules.

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