A1 Journal article (refereed)
The primary structural photoresponse of phytochrome proteins captured by a femtosecond X-ray laser (2020)

Claesson, E., Wahlgren, W. Y., Takala, H., Pandey, S., Castillon, L., Kuznetsova, V., Henry, L., Panman, M., Carrillo, M., Kübel, J., Nanekar, R., Isaksson, L., Nimmrich, A., Cellini, A., Morozov, D., Maj, M., Kurttila, M., Bosman, R., Nango, E., . . . Westenhof, S. (2020). The primary structural photoresponse of phytochrome proteins captured by a femtosecond X-ray laser. eLife, 9, Article e53514. https://doi.org/10.7554/eLife.53514

JYU authors or editors

Takala, Heikki
Kuznetsova, Valentyna
Nanekar, Rahul
Morozov, Dmitry
Kurttila, Moona
Groenhof, Gerrit
Ihalainen, Janne

Publication details

All authors or editors: Claesson, Elin; Wahlgren, Weixiao Yuan; Takala, Heikki; Pandey, Suraj; Castillon, Leticia; Kuznetsova, Valentyna; Henry, Léocadie; Panman, Matthijs; Carrillo, Melissa; Kübel, Joachim; et al.

Journal or series: eLife

eISSN: 2050-084X

Publication year: 2020

Volume: 9

Article number: e53514

Publisher: eLife Sciences Publications

Publication country: United Kingdom

Publication language: English

DOI: https://doi.org/10.7554/eLife.53514

Publication open access: Openly available

Publication channel open access: Open Access channel

Publication is parallel published (JYX): https://jyx.jyu.fi/handle/123456789/68677

Web address of parallel published publication (pre-print): https://www.biorxiv.org/content/10.1101/789305v1

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.

Keywords: photochemistry; proteins; x-ray crystallography

Fields of science: