Pr and Pfr structures of plant phytochrome A
Abstract
Abstract Phytochromes are biliprotein photoreceptors widespread amongst microorganisms and ubiquitous in plants where they control developmental processes as diverse as germination, stem elongation and floral induction through the photoconversion of inactive Pr to the Pfr signalling state. Here we report crystal structures of the chromophore-binding module of soybean phytochrome A, including ~2.2 Å XFEL structures of Pr and Pfr at ambient temperature and high resolution cryogenic structures of Pr. In the Pfr structure, the chromophore is exposed to the medium, the D-ring remaining α-facial following the likely clockwise photoflip. The chromophore shifts within its pocket, while its propionate side chains, their partners as well as three neighbouring tyrosines shift radically. Helices near the chromophore show substantial shifts that might represent components of the light signal. These changes reflect those in bacteriophytochromes despite their quite different signalling mechanisms, implying that fundamental aspects of phytochrome photoactivation have been repurposed for photoregulation in the eukaryotic plant.
Article Details
Authors (32)
Soshichiro Nagano
David von Stetten
Kaoling Guan
Peng-Yuan Chen
Chen Song
Center for Quantitative Biology
Thomas Barends
Manfred S. Weiss
Christian G. Feiler
Katerina Dörner
Iñaki de Diego Martinez
Robin Schubert
Johan Bielecki
Lea Brings
Huijong Han
Konstantin Kharitonov
Chan Kim
Marco Kloos
European X-ray Free Electron Laser, Holzkoppel 4, 22869 Schenefeld, Germany
Jayanath C. P. Koliyadu
Faisal H. M. Koua
Ekaterina Round
Abhisakh Sarma
Tokushi Sato
Christina Schmidt
Forschungszentrum Jülich GmbH, Helmholtz-Institute Münster (IMD-4), Corrensstraße 46, 48149 Münster, Germany
Joana Valerio
European XFEL, Holzkoppel 4, 22869 Schenefeld, Germany
Agnieszka Wrona
Joachim Schulz
Raphael de Wijn
Romain Letrun
Richard Bean
Adrian Mancuso
Karsten Heyne
Jon Hughes