6LZ3

Structure of cryptochrome in active conformation

Summary for 6LZ3

• Entry DOI: 10.2210/pdb6lz3/pdb
• EMDB information: 30022
• Descriptor: Cryptochrome2, FLAVIN-ADENINE DINUCLEOTIDE (2 entities in total)
• Functional Keywords: cryptochrome, photoreceptor, photosignaling, plant protein, flavoprotein
• Biological source: Zea mays (Maize)
• Total number of polymer chains: 4
• Total formula weight: 313578.70

Authors

Shao, K.,Zhang, X.,Zhang, P. (deposition date: 2020-02-18, release date: 2020-04-29, Last modification date: 2020-11-11)

Primary citation

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

Experimental method

ELECTRON MICROSCOPY (3.2 Å)