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Structure. 2017 Jun 6;25(6):933-938.e3. doi: 10.1016/j.str.2017.04.006. Epub 2017 May 11.

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

Author information

1
Department of Chemistry and Molecular Biology, University of Gothenburg, 40530 Gothenburg, Sweden.
2
Department of Biology, Humboldt-Universität zu Berlin, 10115 Berlin, Germany.
3
European Synchrotron Radiation Facility, 38000 Grenoble, France.
4
Paul Scherrer Institut, 5232 Villigen, Switzerland.
5
Center for Advanced Radiation Sources, The University of Chicago, Chicago, IL 60637, USA.
6
Department of Biology, Humboldt-Universität zu Berlin, 10115 Berlin, Germany; Department of Biochemistry, Research Center for Bio-Macromolecules, Universität Bayreuth, 95440 Bayreuth, Germany. Electronic address: andreas.moeglich@uni-bayreuth.de.
7
Department of Chemistry and Molecular Biology, University of Gothenburg, 40530 Gothenburg, Sweden. Electronic address: westenho@chem.gu.se.

Abstract

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.

KEYWORDS:

Light-oxygen-voltage; X-ray solution scattering; photocycle; protein structural dynamics; sensor histidine kinase; sensory photoreceptor; signal transduction

PMID:
28502782
DOI:
10.1016/j.str.2017.04.006
[Indexed for MEDLINE]
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