A light-sensing knot revealed by the structure of the chromophore-binding domain of phytochrome

Jeremiah R. Wagner, Joseph S. Brunzelle, Katrina T. Forest*, Richard D. Vierstra

*Corresponding author for this work

Research output: Contribution to journalArticlepeer-review

394 Scopus citations

Abstract

Phytochromes are red/far-red light photoreceptors that direct photosensory responses across the bacterial, fungal and plant kingdoms. These include photosynthetic potential and pigmentation in bacteria as well as chloroplast development and photomorphogenesis in plants. Phytochromes consist of an amino-terminal region that covalently binds a single bilin chromophore, followed by a carboxy-terminal dimerization domain that often transmits the light signal through a histidine kinase relay. Here we describe the three-dimensional structure of the chromophore-binding domain of Deinococcus radiodurans phytochrome assembled with its chromophore biliverdin in the Pr ground state. Our model, refined to 2.5 Å resolution, reaffirms Cys 24 as the chromophore attachment site, locates key amino acids that form a solvent-shielded bilin-binding pocket, and reveals an unusually formed deep trefoil knot that stabilizes this region. The structure provides the first three-dimensional glimpse into the photochromic behaviour of these photoreceptors and helps to explain the evolution of higher plant phytochromes from prokaryotic precursors.

Original languageEnglish (US)
Pages (from-to)325-331
Number of pages7
JournalNature
Volume438
Issue number7066
DOIs
StatePublished - Nov 17 2005

ASJC Scopus subject areas

  • General

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