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

By Elin Claesson, Weixiao Yuan Wahlgren, Heikki Takala, Suraj Pandey1, Leticia Castillon, Valentyna Kuznetsova, Léocadie Henry, Matthijs Panman, Melissa Carrillo2, Joachim Kübel, Rahul Nanekar, Linnéa Isaksson, Amke Nimmrich, Andrea Cellini, Dmitry Morozov, Michał Maj, Moona Kurttila, Robert William Bosman3, Eriko Nango, Rie Tanaka, Tomoyuki Tanaka, Luo Fangjia, So Iwata, Shigeki Owada, Keith Moffat, Gerrit Groenhof, Emina Stojkovic4, Janne A Ihalainen, Marius Schmidt1, Sebastian Westenhoff

1. University of Wisconsin - Milwaukee 2. Northeastern Illinois Univeristy 3. University of Gothenburg 4. Northern Illinois University

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Type

journal-article

Author

Elin Claesson and Weixiao Yuan Wahlgren and Heikki Takala and Suraj Pandey and Leticia Castillon and Valentyna Kuznetsova and Léocadie Henry and Matthijs Panman and Melissa Carrillo and Joachim Kübel and Rahul Nanekar and Linnéa Isaksson and Amke Nimmrich and Andrea Cellini and Dmitry Morozov and Michał Maj and Moona Kurttila and Robert Bosman and Eriko Nango and Rie Tanaka and Tomoyuki Tanaka and Luo Fangjia and So Iwata and Shigeki Owada and Keith Moffat and Gerrit Groenhof and Emina A. Stojković and Janne A. Ihalainen and Marius Schmidt and Sebastian Westenhoff

Citation

Claesson, E. et al., 2020. The primary structural photoresponse of phytochrome proteins captured by a femtosecond X-ray laser. eLife, 9. Available at: http://dx.doi.org/10.7554/elife.53514.

Abstract

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 signalling 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.

DOI

Funding

NSF-STC Biology with X-ray Lasers (NSF-1231306)