9LPG

Crystal structure of maize CRY-GL2 photosignaling complex

Summary for 9LPG

• Entry DOI: 10.2210/pdb9lpg/pdb
• Descriptor: Cryptochrome2, Protein ECERIFERUM 26-like, FLAVIN-ADENINE DINUCLEOTIDE, ... (4 entities in total)
• Functional Keywords: complex, plant protein
• Biological source: Zea mays; More
• Total number of polymer chains: 4
• Total formula weight: 248525.36

Authors

Liu, Y.,Zhang, P. (deposition date: 2025-01-24, release date: 2025-11-05, Last modification date: 2026-05-27)

Primary citation

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

Experimental method

X-RAY DIFFRACTION (2.8 Å)