Helical rearrangement of photoactivated rhodopsin in monomeric and dimeric forms probed by high-angle X-ray scattering

Yasushi Imamoto, Keiichi Kojima, Toshihiko Oka, Ryo Maeda, Yoshinori Shichida

Research output: Contribution to journalArticle

6 Citations (Scopus)

Abstract

Light-induced helical rearrangement of vertebrate visual rhodopsin was directly monitored by high-angle X-ray scattering (HAXS), ranging from Q (= 4π sin θ/λ) = 0.03 Å-1 to Q = 1.5 Å-1. HAXS of nanodiscs containing a single rhodopsin molecule was performed before and after photoactivation of rhodopsin. The intensity difference curve obtained by HAXS agreed with that calculated from the crystal structure of dark state rhodopsin and metarhodopsin II, indicating that the conformational change of monomeric rhodopsin in the membrane is consistent with that occurring in the crystal. On the other hand, the HAXS intensity difference curve of nanodiscs containing two rhodopsin molecules was significantly reduced, similar to that calculated from the crystal structure of the deprotonated intermediate, without a large conformational change. These results suggest that rhodopsin is dimerized in the membrane and that the interaction between rhodopsin molecules modulates structural changes.

Original languageEnglish
Pages (from-to)1965-1973
Number of pages9
JournalPhotochemical and Photobiological Sciences
Volume14
Issue number11
DOIs
Publication statusPublished - 2015
Externally publishedYes

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Rhodopsin
X ray scattering
scattering
x rays
membranes
molecules
vertebrates
crystal structure
curves
Molecules
Crystal structure
Membranes
crystals
interactions
Crystals

ASJC Scopus subject areas

  • Physical and Theoretical Chemistry

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Helical rearrangement of photoactivated rhodopsin in monomeric and dimeric forms probed by high-angle X-ray scattering. / Imamoto, Yasushi; Kojima, Keiichi; Oka, Toshihiko; Maeda, Ryo; Shichida, Yoshinori.

In: Photochemical and Photobiological Sciences, Vol. 14, No. 11, 2015, p. 1965-1973.

Research output: Contribution to journalArticle

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AB - Light-induced helical rearrangement of vertebrate visual rhodopsin was directly monitored by high-angle X-ray scattering (HAXS), ranging from Q (= 4π sin θ/λ) = 0.03 Å-1 to Q = 1.5 Å-1. HAXS of nanodiscs containing a single rhodopsin molecule was performed before and after photoactivation of rhodopsin. The intensity difference curve obtained by HAXS agreed with that calculated from the crystal structure of dark state rhodopsin and metarhodopsin II, indicating that the conformational change of monomeric rhodopsin in the membrane is consistent with that occurring in the crystal. On the other hand, the HAXS intensity difference curve of nanodiscs containing two rhodopsin molecules was significantly reduced, similar to that calculated from the crystal structure of the deprotonated intermediate, without a large conformational change. These results suggest that rhodopsin is dimerized in the membrane and that the interaction between rhodopsin molecules modulates structural changes.

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