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- W3119783568 abstract "Cryptochromes (CRYs) are evolutionarily conserved photoreceptors that mediate various light-induced responses in bacteria, plants, and animals. Plant cryptochromes govern a variety of critical growth and developmental processes including seed germination, flowering time and entrainment of the circadian clock. CRY's photocycle involves reduction of their flavin adenine dinucleotide (FAD)-bound chromophore, which is completely oxidized in the dark and semi to fully reduced in the light signaling-active state. Despite the progress in characterizing cryptochromes, important aspects of their photochemistry, regulation, and light-induced structural changes remain to be addressed. In this study, we determine the crystal structure of the photosensory domain of Arabidopsis CRY2 in a tetrameric active state. Systematic structure-based analyses of photo-activated and inactive plant CRYs elucidate distinct structural elements and critical residues that dynamically partake in photo-induced oligomerization. Our study offers an updated model of CRYs photoactivation mechanism as well as the mode of its regulation by interacting proteins." @default.
- W3119783568 created "2021-01-18" @default.
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- W3119783568 date "2021-01-04" @default.
- W3119783568 modified "2023-10-08" @default.
- W3119783568 title "Structural insights into photoactivation of plant Cryptochrome-2" @default.
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- W3119783568 doi "https://doi.org/10.1038/s42003-020-01531-x" @default.
- W3119783568 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/7782693" @default.
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