9ER4
Room temperature structure of Glycine max phyA in Pr
9ER4 の概要
エントリーDOI | 10.2210/pdb9er4/pdb |
分子名称 | Phytochrome A-2, PHYCOCYANOBILIN (3 entities in total) |
機能のキーワード | phytochrome, plant protein |
由来する生物種 | Glycine max (soybean) 詳細 |
タンパク質・核酸の鎖数 | 2 |
化学式量合計 | 81230.04 |
構造登録者 | |
主引用文献 | Nagano, S.,von Stetten, D.,Guan, K.,Chen, P.Y.,Song, C.,Barends, T.,Weiss, M.S.,Feiler, C.G.,Dorner, K.,de Diego Martinez, I.,Schubert, R.,Bielecki, J.,Brings, L.,Han, H.,Kharitonov, K.,Kim, C.,Kloos, M.,Koliyadu, J.C.P.,Koua, F.H.M.,Round, E.,Sarma, A.,Sato, T.,Schmidt, C.,Valerio, J.,Wrona, A.,Schulz, J.,de Wijn, R.,Letrun, R.,Bean, R.,Mancuso, A.,Heyne, K.,Hughes, J. Pr and Pfr structures of plant phytochrome A. Nat Commun, 16:5319-5319, 2025 Cited by PubMed 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. PubMed: 40544164DOI: 10.1038/s41467-025-60738-w 主引用文献が同じPDBエントリー |
実験手法 | X-RAY DIFFRACTION (2.2 Å) |
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