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

Authors :
Elin Claesson
Weixiao Yuan Wahlgren
Heikki Takala
Suraj Pandey
Leticia Castillon
Valentyna Kuznetsova
Léocadie Henry
Matthijs Panman
Melissa Carrillo
Joachim Kübel
Rahul Nanekar
Linnéa Isaksson
Amke Nimmrich
Andrea Cellini
Dmitry Morozov
Michał Maj
Moona Kurttila
Robert Bosman
Eriko Nango
Rie Tanaka
Tomoyuki Tanaka
Luo Fangjia
So Iwata
Shigeki Owada
Keith Moffat
Gerrit Groenhof
Emina A Stojković
Janne A Ihalainen
Marius Schmidt
Sebastian Westenhoff
Source :
eLife, Vol 9 (2020)
Publication Year :
2020
Publisher :
eLife Sciences Publications Ltd, 2020.

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 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.

Details

Language :
English
ISSN :
2050084X
Volume :
9
Database :
Directory of Open Access Journals
Journal :
eLife
Publication Type :
Academic Journal
Accession number :
edsdoj.4000fc81ba304ee4ac180eaefc6b63f3
Document Type :
article
Full Text :
https://doi.org/10.7554/eLife.53514