Author
Listed:
- Andrea Schmidt
(Institute for Medical Physics and Biophysics, Group Protein X-ray Crystallography and Signal Transduction)
- Luisa Sauthof
(Institute for Medical Physics and Biophysics, Group Protein X-ray Crystallography and Signal Transduction)
- Michal Szczepek
(Institute for Medical Physics and Biophysics, Group Protein X-ray Crystallography and Signal Transduction)
- Maria Fernandez Lopez
(Technische Universität Berlin, Institut für Chemie)
- Francisco Velazquez Escobar
(Technische Universität Berlin, Institut für Chemie)
- Bilal M. Qureshi
(Institute for Medical Physics and Biophysics, Group Protein X-ray Crystallography and Signal Transduction
King Abdullah University of Science and Technology (KAUST))
- Norbert Michael
(Technische Universität Berlin, Institut für Chemie)
- David Buhrke
(Technische Universität Berlin, Institut für Chemie)
- Tammo Stevens
(Institute for Medical Physics and Biophysics, Group Protein X-ray Crystallography and Signal Transduction)
- Dennis Kwiatkowski
(Institute for Medical Physics and Biophysics, Group Protein X-ray Crystallography and Signal Transduction)
- David Stetten
(European Synchrotron Radiation Facility
European Molecular Biology Laboratory (EMBL))
- Maria Andrea Mroginski
(Technische Universität Berlin, Institut für Chemie)
- Norbert Krauß
(Karlsruhe Institute of Technology (KIT), Botanical Institute)
- Tilman Lamparter
(Karlsruhe Institute of Technology (KIT), Botanical Institute)
- Peter Hildebrandt
(Technische Universität Berlin, Institut für Chemie)
- Patrick Scheerer
(Institute for Medical Physics and Biophysics, Group Protein X-ray Crystallography and Signal Transduction)
Abstract
Phytochromes are modular photoreceptors of plants, bacteria and fungi that use light as a source of information to regulate fundamental physiological processes. Interconversion between the active and inactive states is accomplished by a photoinduced reaction sequence which couples the sensor with the output module. However, the underlying molecular mechanism is yet not fully understood due to the lack of structural data of functionally relevant intermediate states. Here we report the crystal structure of a Meta-F intermediate state of an Agp2 variant from Agrobacterium fabrum. This intermediate, the identity of which was verified by resonance Raman spectroscopy, was formed by irradiation of the parent Pfr state and displays significant reorientations of almost all amino acids surrounding the chromophore. Structural comparisons allow identifying structural motifs that might serve as conformational switch for initiating the functional secondary structure change that is linked to the (de-)activation of these photoreceptors.
Suggested Citation
Andrea Schmidt & Luisa Sauthof & Michal Szczepek & Maria Fernandez Lopez & Francisco Velazquez Escobar & Bilal M. Qureshi & Norbert Michael & David Buhrke & Tammo Stevens & Dennis Kwiatkowski & David , 2018.
"Structural snapshot of a bacterial phytochrome in its functional intermediate state,"
Nature Communications, Nature, vol. 9(1), pages 1-13, December.
Handle:
RePEc:nat:natcom:v:9:y:2018:i:1:d:10.1038_s41467-018-07392-7
DOI: 10.1038/s41467-018-07392-7
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