A molecular movie at 1.8 A resolution displays the photocycle of photoactive yellow protein, a eubacterial blue-light receptor, from nanoseconds to seconds

Zhaochun Ren, B Perman, V Srajer, T Y Teng, C Pradervand, Dominique Bourgeois, Friedrich Schotte, T Ursby, R Kort, Michael Wulff, K. Moffat

Research output: Contribution to JournalArticleAcademicpeer-review

Abstract

The photocycle of the bacterial blue-light photoreceptor, photoactive yellow protein, was stimulated by illumination of single crystals by a 7 ns laser pulse. The molecular events were recorded at high resolution by time-resolved X-ray Laue diffraction as they evolved in real time, from 1 ns to seconds after the laser pulse. The complex structural changes during the photocycle at ambient temperature are displayed in a movie of difference electron density maps relative to the dark state. The step critical to entry into the photocycle is identified as flipping of the carbonyl group of the 4-hydroxycinnamic acid chromophore into an adjacent, hydrophobic environment rather than the concomitant isomerization about the double bond of the chromophore tail. The structural perturbation generated at the chromophore propagates throughout the entire protein as a light-induced "protein quake" with its "epicenter" at the carbonyl moiety of the chromophore.

Original languageEnglish
Pages (from-to)13788-801
Number of pages14
JournalBiochemistry
Volume40
Issue number46
DOIs
Publication statusPublished - 20 Nov 2001

Keywords

  • Bacterial Proteins
  • Computer Simulation
  • Crystallography, X-Ray
  • Halorhodospira halophila
  • Hydrogen Bonding
  • Models, Molecular
  • Oxygen
  • Photoperiod
  • Photoreceptors, Microbial
  • Solutions
  • Thermodynamics
  • Time Factors
  • Comparative Study
  • Journal Article
  • Research Support, U.S. Gov't, P.H.S.

Fingerprint

Dive into the research topics of 'A molecular movie at 1.8 A resolution displays the photocycle of photoactive yellow protein, a eubacterial blue-light receptor, from nanoseconds to seconds'. Together they form a unique fingerprint.

Cite this