Light-induced structural changes in a monomeric bacteriophytochrome
Takala, H., Niebling, S., Berntsson, O., Björling, A., Lehtivuori, H., Häkkänen, H., Panman, M., Gustavsson, E., Hoernke, M., Newby, G., Zontone, F., Wulff, M., Menzel, A., Ihalainen, J., & Westenhoff, S. (2016). Light-induced structural changes in a monomeric bacteriophytochrome. Structural Dynamics, 3(5), Article 054701. https://doi.org/10.1063/1.4961911
Published inStructural Dynamics
DisciplineSolu- ja molekyylibiologiaFysiikkaNanoscience CenterCell and Molecular BiologyPhysicsNanoscience Center
© Author(s) 2016. This is an open access article distributed under the terms of a Creative Commons License.
Phytochromes sense red light in plants and various microorganism. Light absorption causes structural changes within the protein, which alter its biochemical activity. Bacterial phytochromes are dimeric proteins, but the functional relevance of this arrangement remains unclear. Here, we use time-resolved X-ray scattering to reveal the solution structural change of a monomeric variant of the photosensory core module of the phytochrome from Deinococcus radiodurans. The data reveal two motions, a bend and a twist of the PHY domain with respect to the chromophore-binding domains. Infrared spectroscopy shows the refolding of the PHY tongue. We conclude that a monomer of the phytochrome photosensory core is sufficient to perform the light-induced structural changes. This implies that allosteric cooperation with the other monomer is not needed for structural activation. The dimeric arrangement may instead be intrinsic to the biochemical output domains of bacterial phytochromes.
PublisherAmerican Crystallographic Association; AIP Publishing
Publication in research information system
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Except where otherwise noted, this item's license is described as © Author(s) 2016. This is an open access article distributed under the terms of a Creative Commons License.
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