Chromophore conformation and the evolution of tertiary structural changes in photoactive yellow protein

Spencer Anderson*, Vukica Srajer, Reinhard Pahl, Sudarshan Rajagopal, Friedrich Schotte, Philip Anfinrud, Michael Wulff, Keith Moffat

*Corresponding author for this work

Research output: Contribution to journalArticle

54 Scopus citations

Abstract

We use time-resolved crystallography to observe the structural progression of a bacterial blue light photoreceptor throughout its photocycle. Data were collected from 10 ns to 100 ms after photoactivation of the E46Q mutant of photoactive yellow protein. Refinement of transient chromophore conformations shows that the spectroscopically distinct intermediates are formed via progressive disruption of the hydrogen bond network to the chromophore. Although structural change occurs within a few nanoseconds on and around the chromophore, it takes milliseconds for a distinct pattern of tertiary structural change to fully progress through the entire molecule, thus generating the putative signaling state. Remarkably, the coupling between the chromophore conformation and the tertiary structure of this small protein is not tight: there are leads and lags between changes in the conformation of the chromophore and the protein tertiary structure.

Original languageEnglish (US)
Pages (from-to)1039-1045
Number of pages7
JournalStructure
Volume12
Issue number6
DOIs
StatePublished - Jun 1 2004

ASJC Scopus subject areas

  • Structural Biology
  • Molecular Biology

Fingerprint Dive into the research topics of 'Chromophore conformation and the evolution of tertiary structural changes in photoactive yellow protein'. Together they form a unique fingerprint.

  • Cite this

    Anderson, S., Srajer, V., Pahl, R., Rajagopal, S., Schotte, F., Anfinrud, P., Wulff, M., & Moffat, K. (2004). Chromophore conformation and the evolution of tertiary structural changes in photoactive yellow protein. Structure, 12(6), 1039-1045. https://doi.org/10.1016/j.str.2004.04.008