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dc.contributor.author | Imamoto, Yasushi | en |
dc.contributor.author | Kojima, Keiichi | en |
dc.contributor.author | Oka, Toshihiko | en |
dc.contributor.author | Maeda, Ryo | en |
dc.contributor.author | Shichida, Yoshinori | en |
dc.contributor.alternative | 今元, 泰 | ja |
dc.date.accessioned | 2019-11-11T02:54:16Z | - |
dc.date.available | 2019-11-11T02:54:16Z | - |
dc.date.issued | 2019-10-31 | - |
dc.identifier.issn | 1520-6106 | - |
dc.identifier.uri | http://hdl.handle.net/2433/244712 | - |
dc.description.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. | en |
dc.format.mimetype | application/pdf | - |
dc.language.iso | eng | - |
dc.publisher | American Chemical Society (ACS) | en |
dc.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 https://doi.org/10.1021/acs.jpcb.9b08311. | en |
dc.rights | 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'. | en |
dc.rights | This is not the published version. Please cite only the published version. | en |
dc.rights | 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。 | ja |
dc.title | Conformational differences among metarhodopsin I, metarhodopsin II, and opsin probed by wide-angle X-ray scattering | en |
dc.type | journal article | - |
dc.type.niitype | Journal Article | - |
dc.identifier.jtitle | The Journal of Physical Chemistry B | en |
dc.identifier.volume | 123 | - |
dc.identifier.issue | 43 | - |
dc.identifier.spage | 9134 | - |
dc.identifier.epage | 9142 | - |
dc.relation.doi | 10.1021/acs.jpcb.9b08311 | - |
dc.textversion | author | - |
dc.address | Department of Biophysics, Graduate School of Science, Kyoto University | en |
dc.address | Department of Biophysics, Graduate School of Science, Kyoto University | en |
dc.address | Department of Physics, Faculty of Science, Nanomaterials Research Division, Research Institute of Electronics, Shizuoka University | en |
dc.address | Department of Biophysics, Graduate School of Science, Kyoto University | en |
dc.address | Research Organization for Science and Technology, Ritsumeikan University | en |
dc.identifier.pmid | 31580080 | - |
dcterms.accessRights | open access | - |
datacite.date.available | 2020-10-03 | - |
dc.identifier.pissn | 1520-6106 | - |
dc.identifier.eissn | 1520-5207 | - |
出現コレクション: | 学術雑誌掲載論文等 |
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