6X24
Structural basis of plant blue light photoreceptor
Summary for 6X24
| Entry DOI | 10.2210/pdb6x24/pdb |
| Descriptor | Cryptochrome-2, FLAVIN-ADENINE DINUCLEOTIDE, GLYCEROL, ... (4 entities in total) |
| Functional Keywords | cryptochrome, blue-light receptors, cry2, photolyase, fad, signaling photoreceptor, signaling protein |
| Biological source | Arabidopsis thaliana (Mouse-ear cress) |
| Total number of polymer chains | 4 |
| Total formula weight | 233561.67 |
| Authors | Palayam, M.,Ganapathy, J.,Guercio, M.A.,Shabek, N. (deposition date: 2020-05-19, release date: 2020-12-16, Last modification date: 2023-10-18) |
| Primary citation | Palayam, M.,Ganapathy, J.,Guercio, A.M.,Tal, L.,Deck, S.L.,Shabek, N. Structural insights into photoactivation of plant Cryptochrome-2. Commun Biol, 4:28-28, 2021 Cited by PubMed 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. PubMed: 33398020DOI: 10.1038/s42003-020-01531-x PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (3.25 Å) |
Structure validation
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