6X24

Structural basis of plant blue light photoreceptor

6X24 の概要

• エントリーDOI: 10.2210/pdb6x24/pdb
• 分子名称: Cryptochrome-2, FLAVIN-ADENINE DINUCLEOTIDE, GLYCEROL, ... (4 entities in total)
• 機能のキーワード: cryptochrome, blue-light receptors, cry2, photolyase, fad, signaling photoreceptor, signaling protein
• 由来する生物種: Arabidopsis thaliana (Mouse-ear cress)
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 233561.67

構造登録者

Palayam, M.,Ganapathy, J.,Guercio, M.A.,Shabek, N. (登録日: 2020-05-19, 公開日: 2020-12-16, 最終更新日: 2023-10-18)

主引用文献

Palayam, M.,Ganapathy, J.,Guercio, A.M.,Tal, L.,Deck, S.L.,Shabek, N.
Structural insights into photoactivation of plant Cryptochrome-2.
Commun Biol, 4:28-28, 2021

PubMed Abstract: Cryptochromes (CRYs) are evolutionarily conserved photoreceptors that mediate various light-induced responses in bacteria, plants, and animals. Plant cryptochromes govern a variety of critical growth and developmental processes including seed germination, flowering time and entrainment of the circadian clock. CRY's photocycle involves reduction of their flavin adenine dinucleotide (FAD)-bound chromophore, which is completely oxidized in the dark and semi to fully reduced in the light signaling-active state. Despite the progress in characterizing cryptochromes, important aspects of their photochemistry, regulation, and light-induced structural changes remain to be addressed. In this study, we determine the crystal structure of the photosensory domain of Arabidopsis CRY2 in a tetrameric active state. Systematic structure-based analyses of photo-activated and inactive plant CRYs elucidate distinct structural elements and critical residues that dynamically partake in photo-induced oligomerization. Our study offers an updated model of CRYs photoactivation mechanism as well as the mode of its regulation by interacting proteins.

PubMed: 33398020
DOI: 10.1038/s42003-020-01531-x

実験手法

X-RAY DIFFRACTION (3.25 Å)