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Title: Photoactivation of Drosophila melanogaster cryptochrome through sequential conformational transitions

Journal Article · · Science Advances

Cryptochromes are blue-light photoreceptor proteins, which provide input to circadian clocks. The cryptochrome fromDrosophila 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 inDmCry 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 inDmCry depends on pH. Mutation of a conserved histidine, important for the biochemical activity ofDmCry, 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.

Research Organization:
Argonne National Laboratory (ANL), Argonne, IL (United States)
Sponsoring Organization:
USDOE
Grant/Contract Number:
AC02-06CH11357
OSTI ID:
1545869
Journal Information:
Science Advances, Vol. 5, Issue 7; ISSN 2375-2548
Publisher:
AAASCopyright Statement
Country of Publication:
United States
Language:
ENGLISH
Citation Metrics:
Cited by: 25 works
Citation information provided by
Web of Science

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