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

Author

Listed:
  • Jeremiah R. Wagner

    (Department of Genetics)

  • Joseph S. Brunzelle

    (Northwestern University)

  • Katrina T. Forest

    (University of Wisconsin-Madison)

  • Richard D. Vierstra

    (Department of Genetics)

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.

Suggested Citation

  • Jeremiah R. Wagner & Joseph S. Brunzelle & Katrina T. Forest & Richard D. Vierstra, 2005. "A light-sensing knot revealed by the structure of the chromophore-binding domain of phytochrome," Nature, Nature, vol. 438(7066), pages 325-331, November.
    • Handle: RePEc:nat:nature:v:438:y:2005:i:7066:d:10.1038_nature04118
    DOI: 10.1038/nature04118
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    Cited by:

    1. E. Sethe Burgie & Katherine Basore & Michael J. Rau & Brock Summers & Alayna J. Mickles & Vadim Grigura & James A. J. Fitzpatrick & Richard D. Vierstra, 2024. "Signaling by a bacterial phytochrome histidine kinase involves a conformational cascade reorganizing the dimeric photoreceptor," Nature Communications, Nature, vol. 15(1), pages 1-16, December.
    2. Weixiao Yuan Wahlgren & Elin Claesson & Iida Tuure & Sergio Trillo-Muyo & Szabolcs Bódizs & Janne A. Ihalainen & Heikki Takala & Sebastian Westenhoff, 2022. "Structural mechanism of signal transduction in a phytochrome histidine kinase," Nature Communications, Nature, vol. 13(1), pages 1-8, December.
    3. Derren J Heyes & Basile Khara & Michiyo Sakuma & Samantha J O Hardman & Ronan O'Cualain & Stephen E J Rigby & Nigel S Scrutton, 2012. "Ultrafast Red Light Activation of Synechocystis Phytochrome Cph1 Triggers Major Structural Change to Form the Pfr Signalling-Competent State," PLOS ONE, Public Library of Science, vol. 7(12), pages 1-13, December.
    4. Giacomo Salvadori & Veronica Macaluso & Giulia Pellicci & Lorenzo Cupellini & Giovanni Granucci & Benedetta Mennucci, 2022. "Protein control of photochemistry and transient intermediates in phytochromes," Nature Communications, Nature, vol. 13(1), pages 1-10, December.

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