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Rhodopsins are the members of the family of G protein-coupled receptors that have diverged from ligand-binding receptors into photoreceptive pigments. Vertebrate rhodopsins are able to bind the inverse agonist 11-cis-retinal but are unable to bind the agonist all-trans-retinal, indicating that vertebrate rhodopsin changed its binding ability during the course of molecular evolution. Here, we show that unlike vertebrate rhodopsin, amphioxus rhodopsin is still able to bind the agonist all-trans-retinal. The opsin of amphioxus rhodopsin can also bind 11-cis-retinal to form a photoreceptive pigment that can convert to a red-shifted photoproduct through cis-trans isomerization of the chromophore upon photon absorption. The red-shifted photoproduct is the stable G protein activating state. Incubation of the opsin with all-trans-retinal produces a G protein activating state that is spectroscopically and biochemically indistinguishable from the red-shifted photoproduct, indicating that the opsin possesses agonist-binding ability. The opsin exhibits an approximately 50-fold higher affinity for 11-cis-retinal than for all-trans-retinal, and mutational analyses revealed that Trp-265 situated in helix VI is important for the increase in binding affinity to 11-cis-retinal. These properties of amphioxus rhodopsin suggest that an ancestral rhodopsin increased the affinity for 11-cis-retinal by rearrangement of a structure including Trp-265 to act as a photoreceptor. In addition, an additional mechanism was acquired in vertebrate rhodopsin to prevent completely the binding of exogenous all-trans-retinal during molecular evolution.

A rhodopsin exhibiting binding ability to agonist all-trans-retinal