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- W2977763205 abstract "Among the photoproducts of vertebrate rhodopsin, only metarhodopsin II (Meta-II) preferentially adopts the active structure in which transmembrane helices are rearranged. Light-induced helical rearrangement of rhodopsin in membrane-embedded form was directly monitored by wide-angle X-ray scattering (WAXS) using nanodiscs. The change in the WAXS curve for the formation of Meta-II was characterized by a peak at 0.2 Å–1 and a valley at 0.6 Å–1, which were not observed in metarhodopsin I and opsin. However, acid-induced active opsin (Opsin*) showed a 0.2 Å–1 peak, but no 0.6 Å–1 valley. Analyses using the model structures based on the crystal structures of dark state and Meta-II suggest that the outward movement of helix VI occurred in Opsin*. However, the displaced helices III and V in Meta-II resulting from the disruption of cytoplasmic ionic lock were restored in Opsin*, which is likely to destabilize the G-protein-activating structure of opsin." @default.
- W2977763205 created "2019-10-10" @default.
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- W2977763205 date "2019-10-03" @default.
- W2977763205 modified "2023-09-26" @default.
- W2977763205 title "Conformational Differences among Metarhodopsin I, Metarhodopsin II, and Opsin Probed by Wide-Angle X-ray Scattering" @default.
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- W2977763205 doi "https://doi.org/10.1021/acs.jpcb.9b08311" @default.
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