8P4X

FAD_ox bound dark state structure of PdLCry

Summary for 8P4X

• Entry DOI: 10.2210/pdb8p4x/pdb
• EMDB information: 17429
• Descriptor: Putative light-receptive cryptochrome (Fragment), FLAVIN-ADENINE DINUCLEOTIDE, MAGNESIUM ION, ... (4 entities in total)
• Functional Keywords: light-sensitive, circalunar clock, flavoprotein
• Biological source: Platynereis dumerilii (Dumeril's clam worm); More
• Total number of polymer chains: 2
• Total formula weight: 132585.42

Authors

Behrmann, E.,Behrmann, H. (deposition date: 2023-05-23, release date: 2023-11-08, Last modification date: 2024-03-27)

Primary citation

Vu, H.H.,Behrmann, H.,Hanic, M.,Jeyasankar, G.,Krishnan, S.,Dannecker, D.,Hammer, C.,Gunkel, M.,Solov'yov, I.A.,Wolf, E.,Behrmann, E.
A marine cryptochrome with an inverse photo-oligomerization mechanism.
Nat Commun, 14:6918-6918, 2023

PubMed Abstract: Cryptochromes (CRYs) are a structurally conserved but functionally diverse family of proteins that can confer unique sensory properties to organisms. In the marine bristle worm Platynereis dumerilii, its light receptive cryptochrome L-CRY (PdLCry) allows the animal to discriminate between sunlight and moonlight, an important requirement for synchronizing its lunar cycle-dependent mass spawning. Using cryo-electron microscopy, we show that in the dark, PdLCry adopts a dimer arrangement observed neither in plant nor insect CRYs. Intense illumination disassembles the dimer into monomers. Structural and functional data suggest a mechanistic coupling between the light-sensing flavin adenine dinucleotide chromophore, the dimer interface, and the C-terminal tail helix, with a likely involvement of the phosphate binding loop. Taken together, our work establishes PdLCry as a CRY protein with inverse photo-oligomerization with respect to plant CRYs, and provides molecular insights into how this protein might help discriminating the different light intensities associated with sunlight and moonlight.

PubMed: 37903809
DOI: 10.1038/s41467-023-42708-2

Experimental method

ELECTRON MICROSCOPY (2.57 Å)