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Structural snapshot of a bacterial phytochrome in its functional intermediate state

Andrea Schmidt, Luisa Sauthof, Michal Szczepek, Maria Fernandez Lopez, Francisco Velazquez Escobar, Bilal M. Qureshi, Norbert Michael, David Buhrke, Tammo Stevens, Dennis Kwiatkowski, David Stetten, Maria Andrea Mroginski, Norbert Krauß, Tilman Lamparter, Peter Hildebrandt () and Patrick Scheerer ()
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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
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
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

Nature Communications, 2018, vol. 9, issue 1, 1-13

Abstract: 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.

Date: 2018
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Persistent link: https://EconPapers.repec.org/RePEc:nat:natcom:v:9:y:2018:i:1:d:10.1038_s41467-018-07392-7

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DOI: 10.1038/s41467-018-07392-7

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