EMD-17429

Single-particle
2.57 Å
EMD-17429 Deposition: 23/05/2023
Map released: 08/11/2023
Last modified: 27/03/2024
Overview 3D View Sample Experiment Validation Volume Browser Additional data Links
Overview 3D View Sample Experiment Validation Volume Browser Additional data Links

EMD-17429

FAD_ox bound dark state structure of PdLCry

EMD-17429

Single-particle
2.57 Å
EMD-17429 Deposition: 23/05/2023
Map released: 08/11/2023
Last modified: 27/03/2024
Overview 3D View Sample Experiment Validation Volume Browser Additional data Links
Sample Organism: Platynereis dumerilii
Sample: dimeric complex of PdLCry in the dark state
Fitted models: 8p4x (Avg. Q-score: 0.632)

Deposition Authors: Behrmann E , Behrmann H
A marine cryptochrome with an inverse photo-oligomerization mechanism.
PUBMED: 37903809
DOI: doi:10.1038/s41467-023-42708-2
ISSN: 2041-1723
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.