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-Structure paper
Title | Structural insights into the photoactivation of Arabidopsis CRY2. |
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Journal, issue, pages | Nat Plants, Vol. 6, Issue 12, Page 1432-1438, Year 2020 |
Publish date | Nov 16, 2020 |
![]() | Ling Ma / Zeyuan Guan / Qiang Wang / Xuhui Yan / Jing Wang / Zhizheng Wang / Jianbo Cao / Delin Zhang / Xin Gong / Ping Yin / ![]() |
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. ...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. |
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Methods | EM (single particle) |
Resolution | 3.1 Å |
Structure data | EMDB-30128, PDB-6m79: |
Chemicals | ![]() ChemComp-AMP: ![]() ChemComp-FAD: |
Source |
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![]() | TRANSCRIPTION / blue-light activated / Arabidopsis thaliana / CRY2 tetramer |