Retinal orientation and interactions in rhodopsin reveal a two-stage trigger mechanism for activation

Naoki Kimata, Andreyah Pope, Markus Eilers, Chikwado A. Opefi, Martine Ziliox, Amiram Hirshfeld, Ekaterina Zaitseva, Reiner Vogel, Mordechai Sheves, Philip J. Reeves and Steven O. Smith ()
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Naoki Kimata: Stony Brook University
Andreyah Pope: Stony Brook University
Markus Eilers: Stony Brook University
Chikwado A. Opefi: School of Biological Sciences, University of Essex
Martine Ziliox: Stony Brook University
Amiram Hirshfeld: Weizmann Institute
Ekaterina Zaitseva: University of Freiburg, Institute of Physiology II
Reiner Vogel: Biophysics Section, Institute of Molecular Medicine and Cell Research, Albert-Ludwigs-University
Mordechai Sheves: Weizmann Institute
Philip J. Reeves: School of Biological Sciences, University of Essex
Steven O. Smith: Stony Brook University

Nature Communications, 2016, vol. 7, issue 1, 1-10

Abstract: Abstract The 11-cis retinal chromophore is tightly packed within the interior of the visual receptor rhodopsin and isomerizes to the all-trans configuration following absorption of light. The mechanism by which this isomerization event drives the outward rotation of transmembrane helix H6, a hallmark of activated G protein-coupled receptors, is not well established. To address this question, we use solid-state NMR and FTIR spectroscopy to define the orientation and interactions of the retinal chromophore in the active metarhodopsin II intermediate. Here we show that isomerization of the 11-cis retinal chromophore generates strong steric interactions between its β-ionone ring and transmembrane helices H5 and H6, while deprotonation of its protonated Schiff’s base triggers the rearrangement of the hydrogen-bonding network involving residues on H6 and within the second extracellular loop. We integrate these observations with previous structural and functional studies to propose a two-stage mechanism for rhodopsin activation.

Date: 2016
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DOI: 10.1038/ncomms12683

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