Photoactivation of Drosophila melanogaster cryptochrome through sequential conformational transitions

Research output: Contribution to journalArticle


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.


  • Oskar Berntsson
  • Ryan Rodriguez
  • Léocadie Henry
  • Matthijs R. Panman
  • Ashley J. Hughes
  • Christopher Einholz
  • Stefan Weber
  • Janne A. Ihalainen
  • Robert Henning
  • Irina Kosheleva
  • Erik Schleicher
  • Sebastian Westenhoff
External organisations
  • University of Gothenburg
  • Albert-Ludwigs University Freiburg
  • University of Jyväskylä
  • University of Chicago
Research areas and keywords

Subject classification (UKÄ) – MANDATORY

  • Biophysics
Original languageEnglish
Article numbereaaw1531
JournalScience Advances
Issue number7
Publication statusPublished - 2019 Jul 17
Publication categoryResearch