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Photoactivation of Drosophila melanogaster cryptochrome through sequential conformational transitions

Journal article
Authors Oskar Berntsson
R. Rodriguez
Léocadie Henry
Matthijs R Panman
Ashley J Hughes
C. Einholz
S. Weber
J. A. Ihalainen
R. Henning
I. Kosheleva
E. Schleicher
Sebastian Westenhoff
Published in Science Advances
Volume 5
Issue 7
ISSN 2375-2548
Publication year 2019
Published at Department of Chemistry and Molecular Biology
Language en
Keywords blue-light photoreceptors, ray solution scattering, structural dynamics, mechanism, proteins, histidines, Science & Technology
Subject categories Chemical Sciences


Cryptochromes are blue-light photoreceptor proteins, which provide input to circadian clocks. The cryptochrome from Drosophila melanogaster (DmCry) modulates the degradation of Timeless and itself. It is unclear how light absorption by the chromophore and the subsequent redox reactions trigger these events. Here, we use nano- to millisecond time-resolved x-ray solution scattering to reveal the light-activated conformational changes in DmCry and the related (6-4) photolyase. DmCry undergoes a series of structural changes, culminating in the release of the carboxyl-terminal tail (CTT). The photolyase has a simpler structural response. We find that the CTT release in DmCry depends on pH. Mutation of a conserved histidine, important for the biochemical activity of DmCry, does not affect transduction of the structural signal to the CTT. Instead, molecular dynamics simulations suggest that it stabilizes the CTT in the resting-state conformation. Our structural photocycle unravels the first molecular events of signal transduction in an animal cryptochrome.

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