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TitleThe oligomeric structures of plant cryptochromes.
Journal, issue, pagesNat Struct Mol Biol, Vol. 27, Issue 5, Page 480-488, Year 2020
Publish dateMay 11, 2020
AuthorsKai Shao / Xue Zhang / Xu Li / Yahui Hao / Xiaowei Huang / Miaolian Ma / Minhua Zhang / Fang Yu / Hongtao Liu / Peng Zhang /
PubMed AbstractCryptochromes (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 ...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.
External linksNat Struct Mol Biol / PubMed:32398825
MethodsEM (single particle) / X-ray diffraction
Resolution3.2 - 7.2 Å
Structure data

EMDB-30022, PDB-6lz3:
Structure of cryptochrome in active conformation
Method: EM (single particle) / Resolution: 3.2 Å

EMDB-30023:
Tetrameric structure of AtCRY2 PHR domain
Method: EM (single particle) / Resolution: 4.2 Å

EMDB-30024:
ZmCRY1c-PHR dimer
Method: EM (single particle) / Resolution: 7.2 Å

EMDB-30025:
AtCRY2-PHR dimer
Method: EM (single particle) / Resolution: 5.6 Å

PDB-6lz7:
Tetrameric structure of ZmCRY1a PHR domain
Method: X-RAY DIFFRACTION / Resolution: 3.59936165826 Å

Chemicals

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

Source
  • zea mays (maize)
  • Arabidopsis thaliana (thale cress)
KeywordsFLAVOPROTEIN / cryptochrome / photoreceptor / photosignaling / PLANT PROTEIN

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