Structure of archaerhodopsin-2 at 1.8Å resolution

Tsutomu Kouyama, Ryudo Fujii, Soun Kanada, Taichi Nakanishi, Siu Kit Chan, Midori Murakami

    Research output: Contribution to journalArticlepeer-review

    13 Citations (Scopus)

    Abstract

    Archaerhodopsin-2 (aR2), the sole protein found in the claret membrane of Halorubrum sp. Aus-2, functions as a light-driven proton pump. In this study, structural analysis of aR2 was performed using a novel three-dimensional crystal prepared by the successive fusion of claret membranes. The crystal is made up of stacked membranes, in each of which aR2 trimers are arranged on a hexagonal lattice. This lattice structure resembles that found in the purple membrane of H. salinarum, except that lipid molecules trapped within the trimeric structure are not distributed with perfect threefold symmetry. Nonetheless, diffraction data at 1.8Å resolution provide accurate structural information about functionally important residues. It is shown that two glutamates in the proton-release channel form a paired structure that is maintained by a low-barrier hydrogen bond. Although the structure of the proton-release pathway is highly conserved among proton-pumping archaeal rhodopsins, aR2 possesses the following peculiar structural features: (i) the motional freedom of the tryptophan residue that makes contact with the C13 methyl group of retinal is restricted, affecting the formation/decay kinetics of the L state, and (ii) the N-terminal polypeptide folds into an Ω-loop, which may play a role in organizing the higher-order structure.

    Original languageEnglish
    Pages (from-to)2692-2701
    Number of pages10
    JournalActa Crystallographica Section D: Biological Crystallography
    Volume70
    Issue number10
    DOIs
    Publication statusPublished - Sep 30 2014

    Keywords

    • archaerhodopsin-2
    • light-driven proton pump

    ASJC Scopus subject areas

    • Structural Biology

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