8Z1J

SFX structure of dark adapted CraCRY

Summary for 8Z1J

• Entry DOI: 10.2210/pdb8z1j/pdb
• Descriptor: Animal-like cryptochrome, FLAVIN-ADENINE DINUCLEOTIDE, CHLORIDE ION, ... (4 entities in total)
• Functional Keywords: photoreceptor, flavoprotein, time-resolved crystallography, resting state
• Biological source: Chlamydomonas reinhardtii CC3269
• Total number of polymer chains: 1
• Total formula weight: 58628.07

Authors

Maestre-Reyna, M.,Hosokawa, Y.,Wang, P.-H.,Saft, M.,Caramello, N.,Engilberge, S.,Franz-Badur, S.,Ngura Putu, E.P.G.,Nakamura, M.,Wu, W.-J.,Wu, H.-Y.,Lee, C.-C.,Huang, W.-C.,Huang, K.-F.,Chang, Y.-K.,Yang, C.-H.,Lin, W.-T.,Yang, K.-C.,Ban, Y.,Imura, T.,Kazuoka, A.,Tanida, E.,Owada, S.,Joti, Y.,Tanaka, R.,Tanaka, T.,Luo, F.,Tono, K.,Kiontke, S.,Korf, L.,Umena, Y.,Tosha, T.,Bessho, Y.,Nango, E.,Iwata, S.,Royant, A.,Tsai, M.-D.,Yamamoto, J.,Essen, L.-O. (deposition date: 2024-04-11, release date: 2025-05-14, Last modification date: 2025-05-28)

Primary citation

Maestre-Reyna, M.,Hosokawa, Y.,Wang, P.H.,Saft, M.,Caramello, N.,Engilberge, S.,Franz-Badur, S.,Gusti Ngurah Putu, E.P.,Nakamura, M.,Wu, W.J.,Wu, H.Y.,Lee, C.C.,Huang, W.C.,Huang, K.F.,Chang, Y.K.,Yang, C.H.,Fong, M.I.,Lin, W.T.,Yang, K.C.,Ban, Y.,Imura, T.,Kazuoka, A.,Tanida, E.,Owada, S.,Joti, Y.,Tanaka, R.,Tanaka, T.,Kang, J.,Luo, F.,Tono, K.,Kiontke, S.,Korf, L.,Umena, Y.,Tosha, T.,Bessho, Y.,Nango, E.,Iwata, S.,Royant, A.,Tsai, M.D.,Yamamoto, J.,Essen, L.O.
Capturing structural intermediates in an animal-like cryptochrome photoreceptor by time-resolved crystallography.
Sci Adv, 11:eadu7247-eadu7247, 2025

PubMed Abstract: Animal-like cryptochromes are photoreceptors that control circadian rhythm and signaling in many eukaryotes. Transient photoreduction of the cryptochrome flavin chromophore initiated signaling via a poorly understood mechanism. By serial femtosecond crystallography (SFX), we show that the photoreduction mechanism of cryptochrome involves three loci [carboxyl-terminal region, a transient protonation pathway, and flavin adenine dinucleotide (FAD)-binding site] acting in unison to accomplish three effects: radical pair stabilization, protonation of FAD radical, and formation of the signaling state. Using 19 time-resolved SFX snapshots between 10 nanoseconds and 233 milliseconds, we found that light-driven FAD/tyrosyl-373 radical pair (RP) formation primes α22 unfolding. Electron transfer-dependent protonation of aspartate-321 by tyrosine-373 is the epicenter of unfolding by disrupting salt bridges between α22 and the photolyase homology region. Before helix unfolding, another pathway opens transiently for FAD protonation and RP stabilization. This link between RP formation and conformational changes provides a structural basis for signaling by animal-like cryptochromes.

PubMed: 40378212
DOI: 10.1126/sciadv.adu7247

Experimental method

X-RAY DIFFRACTION (1.64 Å)