EMD-17429
FAD_ox bound dark state structure of PdLCry
EMD-17429
Single-particle2.57 Å
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Map released: 08/11/2023
Last modified: 27/03/2024
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
Sample: dimeric complex of PdLCry in the dark state
Fitted models: 8p4x (Avg. Q-score: 0.632)
Deposition Authors: Behrmann E
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A marine cryptochrome with an inverse photo-oligomerization mechanism.
Vu HH
,
Behrmann H,
Hanic M,
Jeyasankar G,
Krishnan S,
Dannecker D
,
Hammer C
,
Gunkel M
,
Solov'yov IA
,
Wolf E
,
Behrmann E
(2023) Nat Commun , 14 , 6918 - 6918
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(2023) Nat Commun , 14 , 6918 - 6918
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.
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.