The primary structural photoresponse of phytochrome proteins captured by a femtosecond X-ray laser

eLife

Keith Moffat¹  Rahul Nanekar²  Janne A Ihalainen²  Valentyna Kuznetsova²  Moona Kurttila²  Heikki Takala³  Melissa Carrillo⁴  Emina A Stojković⁴  Tomoyuki Tanaka⁵  Luo Fangjia⁵  Rie Tanaka⁵  Eriko Nango⁵  So Iwata⁵  Linnéa Isaksson⁶  Sebastian Westenhoff⁶  Léocadie Henry⁶  Leticia Castillon⁶  Matthijs Panman⁶  Michał Maj⁶  Robert Bosman⁶  Weixiao Yuan Wahlgren⁶  Andrea Cellini⁶  Joachim Kübel⁶  Elin Claesson⁶  Amke Nimmrich⁶  Dmitry Morozov⁷  Gerrit Groenhof⁷  Marius Schmidt⁸  Suraj Pandey⁸  Shigeki Owada⁹ 

[1] Department of Biochemistry and Molecular Biology and Institute for Biophysical Dynamics, University of Chicago, Chicago, United States;Department of Biological and Environmental Science, Nanoscience Center, University of Jyvaskyla, Jyvaskyla, Finland;Department of Biological and Environmental Science, Nanoscience Center, University of Jyvaskyla, Jyvaskyla, Finland;Department of Anatomy, Faculty of Medicine, University of Helsinki, Helsinki, Finland;Department of Biology, Northeastern Illinois University, Chicago, United States;Department of Cell Biology, Graduate School of Medicine, Kyoto University, Kyoto, Japan;RIKEN SPring-8 Center, Hyogo, Japan;Department of Chemistry and Molecular Biology, University of Gothenburg, Gothenburg, Sweden;Department of Chemistry, Nanoscience Center, University of Jyvaskyla, Jyvaskyla, Finland;Physics Department, University of Wisconsin-Milwaukee, Milwaukee, United States;RIKEN SPring-8 Center, Hyogo, Japan;Japan Synchrotron Radiation Research Institute, Hyogo, Japan;

关键词: phytochromes;    SFX;    Deinococcus radiodurans;    initial photorespons;    Other;   

DOI  :  10.7554/eLife.53514

来源: publisher

【 摘 要 】

Phytochrome proteins control the growth, reproduction, and photosynthesis of plants, fungi, and bacteria. Light is detected by a bilin cofactor, but it remains elusive how this leads to activation of the protein through structural changes. We present serial femtosecond X-ray crystallographic data of the chromophore-binding domains of a bacterial phytochrome at delay times of 1 ps and 10 ps after photoexcitation. The data reveal a twist of the D-ring, which leads to partial detachment of the chromophore from the protein. Unexpectedly, the conserved so-called pyrrole water is photodissociated from the chromophore, concomitant with movement of the A-ring and a key signaling aspartate. The changes are wired together by ultrafast backbone and water movements around the chromophore, channeling them into signal transduction towards the output domains. We suggest that the observed collective changes are important for the phytochrome photoresponse, explaining the earliest steps of how plants, fungi and bacteria sense red light.

【 授权许可】

CC BY