Light-induced structural changes in a monomeric bacteriophytochrome.
- Takala H Department of Chemistry and Molecular Biology, University of Gothenburg , Gothenburg 40530, Sweden.
- Niebling S Department of Chemistry and Molecular Biology, University of Gothenburg , Gothenburg 40530, Sweden.
- Berntsson O Department of Chemistry and Molecular Biology, University of Gothenburg , Gothenburg 40530, Sweden.
- Björling A Nanoscience Center, Department of Biological and Environmental Sciences, University of Jyvaskyla , Jyväskylä 40014, Finland.
- Lehtivuori H Department of Chemistry and Molecular Biology, University of Gothenburg , Gothenburg 40530, Sweden.
- Häkkänen H Department of Chemistry and Molecular Biology, University of Gothenburg , Gothenburg 40530, Sweden.
- Panman M ESRF-The European Synchrotron Radiation Facility , CS40220, 38043 Grenoble Cedex 9, France.
- Gustavsson E ESRF-The European Synchrotron Radiation Facility , CS40220, 38043 Grenoble Cedex 9, France.
- Hoernke M ESRF-The European Synchrotron Radiation Facility , CS40220, 38043 Grenoble Cedex 9, France.
- Newby G Paul Scherrer Institut , 5232 Villigen PSI, Switzerland.
- Zontone F Nanoscience Center, Department of Biological and Environmental Sciences, University of Jyvaskyla , Jyväskylä 40014, Finland.
- Wulff M Department of Chemistry and Molecular Biology, University of Gothenburg , Gothenburg 40530, Sweden.
- Menzel A
- Ihalainen JA
- Westenhoff S
- 2016-09-29
Published in:
- Structural dynamics (Melville, N.Y.). - 2016
English
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.
- Language
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- English
- Open access status
- gold
- Identifiers
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- DOI 10.1063/1.4961911
- PMID 27679804
- Persistent URL
- https://sonar.ch/global/documents/92932
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