9LPG

Crystal structure of maize CRY-GL2 photosignaling complex

9LPG の概要

• エントリーDOI: 10.2210/pdb9lpg/pdb
• 分子名称: Cryptochrome2, Protein ECERIFERUM 26-like, FLAVIN-ADENINE DINUCLEOTIDE, ... (4 entities in total)
• 機能のキーワード: complex, plant protein
• 由来する生物種: Zea mays; 詳細
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 248525.36

構造登録者

Liu, Y.,Zhang, P. (登録日: 2025-01-24, 公開日: 2025-11-05, 最終更新日: 2026-05-27)

主引用文献

Liu, Y.,Zhao, Z.,Zhang, X.,Hao, Y.,Feng, F.,Chen, Y.,Wang, J.,Ma, M.,Li, J.,Yu, F.,Liu, H.,Zhang, P.
Structural assembly of maize CRY-GL2 photosignaling complex provides insights into its regulatory role in cuticular wax biosynthesis.
Sci Adv, 11:eadz0136-eadz0136, 2025

PubMed Abstract: Plant cryptochromes (CRYs) are blue-light photoreceptors regulating physiological processes via oligomerization-dependent interaction with effectors. However, the structural basis for photoactivated CRY-effector assembly remains elusive. Here, we report the crystal structure of an active maize CRY1c photolyase homology region in complex with GLOSSY2 (ZmGL2), a BAHD acyltransferase family protein that could form an enzyme complex with ECERIFERUM6 (ZmCER6) and direct very-long-chain fatty acid elongation in cuticular wax biosynthesis. Light-activated CRY1c forms a homotetrameric scaffold. Each protomer binds one ZmGL2 molecule via conformational changes, forming a 4:4 hetero-octameric photosignaling complex. Structural alignment shows 78% overlap between the GL2-binding interfaces in the ZmCRY1c-ZmGL2 and ZmCER6-ZmGL2 complexes. Biochemically, CRY1c dose-dependently inhibits ZmCER6-ZmGL2 enzyme activity, unveiling a light-dependent regulatory switch modulating very-long-chain fatty acid elongation efficiency. Our work establishes the atomic model for light-activated CRY-effector assembly and uncovers spatial competition between photoreceptor and metabolic enzyme complexes as a photoregulatory paradigm in wax biosynthesis.

PubMed: 41337597
DOI: 10.1126/sciadv.adz0136

実験手法

X-RAY DIFFRACTION (2.8 Å)