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

doi:10.1016/S0969-2126(02)00736-0

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

Neuroscience & Cell

Research output: Contribution to journal › Article

49 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 language	English (US)
Pages (from-to)	473-482
Number of pages	10
Journal	Structure
Volume	10
Issue number	4
DOIs	https://doi.org/10.1016/S0969-2126(02)00736-0
State	Published - Apr 23 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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Edman, K., Royant, A., Nollert, P., Maxwell, C. A., Pebay-Peyroula, E., Navarro, J., Neutze, R., & Landau, E. M. (2002). Early structural rearrangements in the photocycle of an integral membrane sensory receptor. Structure, 10(4), 473-482. https://doi.org/10.1016/S0969-2126(02)00736-0

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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 {\AA} 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.",

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AU - Edman, Karl

AU - Royant, Antoine

AU - Nollert, Peter

AU - Maxwell, Carrie A.

AU - Pebay-Peyroula, Eva

AU - Navarro, Javier

AU - Neutze, Richard

AU - Landau, Ehud M.

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AB - 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.

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KW - Kinetic crystallography

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KW - Signal transduction

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KW - Structural mechanism

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