Pr and Pfr structures of plant phytochrome A

Soshichiro Nagano, David Stetten, Kaoling Guan, Peng-Yuan Chen, Chen Song, Thomas Barends, Manfred S. Weiss, Christian G. Feiler, Katerina Dörner, Iñaki Diego Martinez, Robin Schubert, Johan Bielecki, Lea Brings, Huijong Han, Konstantin Kharitonov, Chan Kim, Marco Kloos, Jayanath C. P. Koliyadu, Faisal H. M. Koua, Ekaterina Round, Abhisakh Sarma, Tokushi Sato, Christina Schmidt, Joana Valerio, Agnieszka Wrona, Joachim Schulz, Raphael Wijn, Romain Letrun, Richard Bean, Adrian Mancuso, Karsten Heyne and Jon Hughes ()
Additional contact information
Soshichiro Nagano: Justus Liebig University
David Stetten: European Molecular Biology Laboratory (EMBL)
Kaoling Guan: Justus Liebig University
Peng-Yuan Chen: Justus Liebig University
Chen Song: University of Leipzig
Thomas Barends: Max Planck Institute for Medical Research
Manfred S. Weiss: Macromolecular Crystallography
Christian G. Feiler: Macromolecular Crystallography
Katerina Dörner: European XFEL GmbH
Iñaki Diego Martinez: European XFEL GmbH
Robin Schubert: European XFEL GmbH
Johan Bielecki: European XFEL GmbH
Lea Brings: European XFEL GmbH
Huijong Han: European XFEL GmbH
Konstantin Kharitonov: European XFEL GmbH
Chan Kim: European XFEL GmbH
Marco Kloos: European XFEL GmbH
Jayanath C. P. Koliyadu: European XFEL GmbH
Faisal H. M. Koua: European XFEL GmbH
Ekaterina Round: European XFEL GmbH
Abhisakh Sarma: European XFEL GmbH
Tokushi Sato: European XFEL GmbH
Christina Schmidt: European XFEL GmbH
Joana Valerio: European XFEL GmbH
Agnieszka Wrona: European XFEL GmbH
Joachim Schulz: European XFEL GmbH
Raphael Wijn: European XFEL GmbH
Romain Letrun: European XFEL GmbH
Richard Bean: European XFEL GmbH
Adrian Mancuso: European XFEL GmbH
Karsten Heyne: Free University of Berlin
Jon Hughes: Justus Liebig University

Nature Communications, 2025, vol. 16, issue 1, 1-12

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.

Date: 2025
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Persistent link: https://EconPapers.repec.org/RePEc:nat:natcom:v:16:y:2025:i:1:d:10.1038_s41467-025-60738-w

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DOI: 10.1038/s41467-025-60738-w

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