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TitleStructural insights into the photoactivation of Arabidopsis CRY2.
Journal, issue, pagesNat Plants, Vol. 6, Issue 12, Page 1432-1438, Year 2020
Publish dateNov 16, 2020
AuthorsLing Ma / Zeyuan Guan / Qiang Wang / Xuhui Yan / Jing Wang / Zhizheng Wang / Jianbo Cao / Delin Zhang / Xin Gong / Ping Yin /
PubMed AbstractThe 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.
External linksNat Plants / PubMed:33199893
MethodsEM (single particle)
Resolution3.1 Å
Structure data

30128

6m79

EMDB-30128, PDB-6m79:
Cryo-EM structure of Arabidopsis CRY under blue light-mediated activation
Method: EM (single particle) / Resolution: 3.1 Å

Chemicals

ChemComp-AMP:
ADENOSINE MONOPHOSPHATE / AMP*YM

ChemComp-FAD:
FLAVIN-ADENINE DINUCLEOTIDE / FAD*YM

Source
  • arabidopsis thaliana (thale cress)
KeywordsTRANSCRIPTION / blue-light activated / Arabidopsis thaliana / CRY2 tetramer

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