6LZ7

Tetrameric structure of ZmCRY1a PHR domain

6LZ7 の概要

• エントリーDOI: 10.2210/pdb6lz7/pdb
• 分子名称: Cryptochrome-1, FLAVIN-ADENINE DINUCLEOTIDE (2 entities in total)
• 機能のキーワード: cryptochrome, photoreceptor, photosignaling, plant protein
• 由来する生物種: Zea mays (Maize)
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 58584.73

構造登録者

Shao, K.,Zhang, X.,Zhang, P. (登録日: 2020-02-18, 公開日: 2020-05-13, 最終更新日: 2024-10-30)

主引用文献

Shao, K.,Zhang, X.,Li, X.,Hao, Y.,Huang, X.,Ma, M.,Zhang, M.,Yu, F.,Liu, H.,Zhang, P.
The oligomeric structures of plant cryptochromes.
Nat.Struct.Mol.Biol., 27:480-488, 2020

PubMed Abstract: Cryptochromes (CRYs) are a group of evolutionarily conserved flavoproteins found in many organisms. In plants, the well-studied CRY photoreceptor, activated by blue light, plays essential roles in plant growth and development. However, the mechanism of activation remains largely unknown. Here, we determined the oligomeric structures of the blue-light-perceiving PHR domain of Zea mays CRY1 and an Arabidopsis CRY2 constitutively active mutant. The structures form dimers and tetramers whose functional importance is examined in vitro and in vivo with Arabidopsis CRY2. Structure-based analysis suggests that blue light may be perceived by CRY to cause conformational changes, whose precise nature remains to be determined, leading to oligomerization that is essential for downstream signaling. This photoactivation mechanism may be widely used by plant CRYs. Our study reveals a molecular mechanism of plant CRY activation and also paves the way for design of CRY as a more efficient optical switch.

PubMed: 32398825
DOI: 10.1038/s41594-020-0420-x

実験手法

X-RAY DIFFRACTION (3.59936165826 Å)