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Structural basis for reversible photoswitching in Dronpa.

Martin Andresen1, Andre C Stiel, Simon Trowitzsch

  • 1Department of NanoBiophotonics, Max Planck Institute for Biophysical Chemistry, Am Fassberg 11, 37077 Göttingen, Germany.

Proceedings of the National Academy of Sciences of the United States of America
|July 25, 2007
PubMed
Summary

Dronpa, a fluorescent protein, can be reversibly switched on and off with light. Its dark-state structure reveals chromophore isomerization and amino acid rearrangements, explaining the light-controlled switching mechanism.

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Area of Science:

  • Biochemistry
  • Structural Biology
  • Biophysics

Background:

  • Dronpa is a GFP-like fluorescent protein known for its light-controlled switching capabilities.
  • It reversibly transitions between fluorescent and nonfluorescent states upon light exposure.

Purpose of the Study:

  • To determine the dark-state structure of Dronpa.
  • To elucidate the molecular mechanism underlying its light-induced photoswitching.

Main Methods:

  • Generation of reversibly switchable Dronpa protein crystals.
  • X-ray crystallography to determine the dark-state structure at 1.95-Å resolution.

Main Results:

  • The dark-state structure revealed a cis-trans isomerization of the chromophore.
  • Four neighboring amino acid residues underwent significant structural rearrangements.
  • These rearrangements alter the chromophore's electrostatic environment and protonation state.

Conclusions:

  • A comprehensive model for Dronpa's light-induced switching is proposed.
  • The mechanism involves a cascade of structural changes and altered chromophore protonation states.