Crystal structure of cruxrhodopsin-3 from haloarcula vallismortis

Siu-Kit Chan, Tomomi Kitajima-Ihara, Ryudoh Fujii, Toshiaki Gotoh, Midori Murakami, Kunio Ihara, Tsutomu Kouyama

Research output: Contribution to journalArticle

7 Citations (Scopus)

Abstract

Cruxrhodopsin-3 (cR3), a retinylidene protein found in the claret membrane of Haloarcula vallismortis, functions as a lightdriven proton pump. In this study, the membrane fusion method was applied to crystallize cR3 into a crystal belonging to space group P321. Diffraction data at 2.1 A resolution show that cR3 forms a trimeric assembly with bacterioruberin bound to the crevice between neighboring subunits. Although the structure of the proton-release pathway is conserved among proton-pumping archaeal rhodopsins, cR3 possesses the following peculiar structural features: 1) The DE loop is long enough to interact with a neighboring subunit, strengthening the trimeric assembly; 2) Three positive charges are distributed at the cytoplasmic end of helix F, affecting the higher order structure of cR3; 3) The cytoplasmic vicinity of retinal is more rigid in cR3 than in bacteriorhodopsin, affecting the early reaction step in the proton-pumping cycle; 4) the cytoplasmic part of helix E is greatly bent, influencing the proton uptake process. Meanwhile, it was observed that the photobleaching of retinal, which scarcely occurred in the membrane state, became significant when the trimeric assembly of cR3 was dissociated into monomers in the presence of an excess amount of detergent. On the basis of these observations, we discuss structural factors affecting the photostabilities of ion-pumping rhodopsins.

Original languageEnglish
Article numbere108362
JournalPLoS One
Volume9
Issue number9
DOIs
Publication statusPublished - Sep 30 2014
Externally publishedYes

Fingerprint

Haloarcula
crystal structure
protons
Protons
Crystal structure
rhodopsin
Membranes
Microbial Rhodopsins
Photobleaching
Bacteriorhodopsins
Proton Pumps
photobleaching
proton pump
Membrane Fusion
Rhodopsin
photostability
detergents
Detergents
crystals
Fusion reactions

ASJC Scopus subject areas

  • Medicine(all)
  • Biochemistry, Genetics and Molecular Biology(all)
  • Agricultural and Biological Sciences(all)

Cite this

Chan, S-K., Kitajima-Ihara, T., Fujii, R., Gotoh, T., Murakami, M., Ihara, K., & Kouyama, T. (2014). Crystal structure of cruxrhodopsin-3 from haloarcula vallismortis. PLoS One, 9(9), [e108362]. https://doi.org/10.1371/journal.pone.0108362

Crystal structure of cruxrhodopsin-3 from haloarcula vallismortis. / Chan, Siu-Kit; Kitajima-Ihara, Tomomi; Fujii, Ryudoh; Gotoh, Toshiaki; Murakami, Midori; Ihara, Kunio; Kouyama, Tsutomu.

In: PLoS One, Vol. 9, No. 9, e108362, 30.09.2014.

Research output: Contribution to journalArticle

Chan, S-K, Kitajima-Ihara, T, Fujii, R, Gotoh, T, Murakami, M, Ihara, K & Kouyama, T 2014, 'Crystal structure of cruxrhodopsin-3 from haloarcula vallismortis', PLoS One, vol. 9, no. 9, e108362. https://doi.org/10.1371/journal.pone.0108362
Chan S-K, Kitajima-Ihara T, Fujii R, Gotoh T, Murakami M, Ihara K et al. Crystal structure of cruxrhodopsin-3 from haloarcula vallismortis. PLoS One. 2014 Sep 30;9(9). e108362. https://doi.org/10.1371/journal.pone.0108362
Chan, Siu-Kit ; Kitajima-Ihara, Tomomi ; Fujii, Ryudoh ; Gotoh, Toshiaki ; Murakami, Midori ; Ihara, Kunio ; Kouyama, Tsutomu. / Crystal structure of cruxrhodopsin-3 from haloarcula vallismortis. In: PLoS One. 2014 ; Vol. 9, No. 9.
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