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 › peer-review

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

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title = "Early structural rearrangements in the photocycle of an integral membrane sensory receptor",

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.",

keywords = "Archael rhodopsins, Kinetic crystallography, Sensory rhodopsin II, Signal transduction, Structural intermediates, Structural mechanism",

author = "Karl Edman and Antoine Royant and Peter Nollert and Maxwell, {Carrie A.} and Eva Pebay-Peyroula and Javier Navarro and Richard Neutze and Landau, {Ehud M.}",

note = "Funding Information: We thank D. Bourgeois, J. McCarthy, and E. Mitchell for experimental contributions. Support from the Swedish Science Research Council (VR), SWEGENE, the Swedish Strategic Research Foundation (SSF), The French Ministry of Education and Research (MENR), The Welch Foundation, and the Howard Hughes Medical Institute is greatly acknowledged. J.N. was recipient of an NIH Fogarty International Fellowship. P.N. is a fellow of the Human Frontiers Research Science Organization. ",

year = "2002",

doi = "10.1016/S0969-2126(02)00736-0",

language = "English (US)",

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T1 - Early structural rearrangements in the photocycle of an integral membrane sensory receptor

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.

N1 - Funding Information: We thank D. Bourgeois, J. McCarthy, and E. Mitchell for experimental contributions. Support from the Swedish Science Research Council (VR), SWEGENE, the Swedish Strategic Research Foundation (SSF), The French Ministry of Education and Research (MENR), The Welch Foundation, and the Howard Hughes Medical Institute is greatly acknowledged. J.N. was recipient of an NIH Fogarty International Fellowship. P.N. is a fellow of the Human Frontiers Research Science Organization.

PY - 2002

Y1 - 2002

N2 - 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.

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.

KW - Archael rhodopsins

KW - Kinetic crystallography

KW - Sensory rhodopsin II

KW - Signal transduction

KW - Structural intermediates

KW - Structural mechanism

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

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