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Title: Conformational differences among metarhodopsin I, metarhodopsin II, and opsin probed by wide-angle X-ray scattering
Authors: Imamoto, Yasushi  kyouindb  KAKEN_id  orcid (unconfirmed)
Kojima, Keiichi
Oka, Toshihiko
Maeda, Ryo
Shichida, Yoshinori
Author's alias: 今元, 泰
Issue Date: 31-Oct-2019
Publisher: American Chemical Society (ACS)
Journal title: The Journal of Physical Chemistry B
Volume: 123
Issue: 43
Start page: 9134
End page: 9142
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.
Rights: This document is the Accepted Manuscript version of a Published Work that appeared in final form in The Journal of Physical Chemistry B, copyright © American Chemical Society after peer review and technical editing by the publisher. To access the final edited and published work see
The full-text file will be made open to the public on 3 October 2020 in accordance with publisher's 'Terms and Conditions for Self-Archiving'.
This is not the published version. Please cite only the published version. この論文は出版社版でありません。引用の際には出版社版をご確認ご利用ください。
DOI(Published Version): 10.1021/acs.jpcb.9b08311
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