6M79
Cryo-EM structure of Arabidopsis CRY under blue light-mediated activation
Summary for 6M79
| Entry DOI | 10.2210/pdb6m79/pdb |
| EMDB information | 30128 |
| Descriptor | Cryptochrome-2, ADENOSINE MONOPHOSPHATE, FLAVIN-ADENINE DINUCLEOTIDE (3 entities in total) |
| Functional Keywords | blue-light activated, arabidopsis thaliana, cry2 tetramer, transcription |
| Biological source | Arabidopsis thaliana (Mouse-ear cress) |
| Total number of polymer chains | 4 |
| Total formula weight | 282850.80 |
| Authors | Ma, L.,Guan, Z.Y.,Yin, P. (deposition date: 2020-03-18, release date: 2020-10-14, Last modification date: 2025-09-17) |
| Primary citation | Ma, L.,Guan, Z.,Wang, Q.,Yan, X.,Wang, J.,Wang, Z.,Cao, J.,Zhang, D.,Gong, X.,Yin, P. Structural insights into the photoactivation of Arabidopsis CRY2. Nat.Plants, 6:1432-1438, 2020 Cited by PubMed Abstract: The blue-light receptor cryptochrome (CRY) in plants undergoes oligomerization to transduce blue-light signals after irradiation, but the corresponding molecular mechanism remains poorly understood. Here, we report the cryogenic electron microscopy structure of a blue-light-activated CRY2 tetramer at a resolution of 3.1 Å, which shows how the CRY2 tetramer assembles. Our study provides insights into blue-light-mediated activation of CRY2 and a theoretical basis for developing regulators of CRYs for optogenetic manipulation. PubMed: 33199893DOI: 10.1038/s41477-020-00800-1 PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (3.1 Å) |
Structure validation
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