Early structural rearrangements in the photocycle of an integral membrane sensory receptor

Karl Edman, Antoine Royant, Peter Nollert, Carrie A. Maxwell, Eva Pebay-Peyroula, Javier Navarro, Richard Neutze, Ehud M. Landau

    Research output: Contribution to journalArticlepeer-review

    52 Scopus citations

    Abstract

    Sensory rhodopsins are the primary receptors of vision in animals and phototaxis in microorganisms. Light triggers the rapid isomerization of a buried retinal chromophore, which the protein both accommodates and amplifies into the larger structural rearrangements required for signaling. We trapped an early intermediate of the photocycle of sensory rhodopsin II from Natronobacterium pharaonis (pSRII) in 3D crystals and determined its X-ray structure to 2.3 Å resolution. The observed structural rearrangements were localized near the retinal chromophore, with a key water molecule becoming disordered and the retinal's β-ionone ring undergoing a prominent movement. Comparison with the early structural rearrangements of bacteriorhodopsin illustrates how modifications in the retinal binding pocket of pSRII allow subtle differences in the early relaxation of photoisomerized retinal.

    Original languageEnglish (US)
    Pages (from-to)473-482
    Number of pages10
    JournalStructure
    Volume10
    Issue number4
    DOIs
    StatePublished - 2002

    Keywords

    • Archael rhodopsins
    • Kinetic crystallography
    • Sensory rhodopsin II
    • Signal transduction
    • Structural intermediates
    • Structural mechanism

    ASJC Scopus subject areas

    • Structural Biology
    • Molecular Biology

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