Cryo-EM structure of a Ca2+-bound photosynthetic LH1-RC complex containing multiple αβ-polypeptides

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作者
Kazutoshi Tani
Ryo Kanno
Yuki Makino
Malgorzata Hall
Mizuki Takenouchi
Michie Imanishi
Long-Jiang Yu
Jörg Overmann
Michael T. Madigan
Yukihiro Kimura
Akira Mizoguchi
Bruno M. Humbel
Zheng-Yu Wang-Otomo
机构
[1] Mie University,Graduate School of Medicine
[2] Imaging Section,Department of Agrobioscience
[3] Research Support Division,Faculty of Life Science, Institute of Microbiology
[4] Okinawa Institute of Science and Technology Graduate University (OIST),Department of Microbiology
[5] Faculty of Science,undefined
[6] Ibaraki University,undefined
[7] Graduate School of Agriculture,undefined
[8] Kobe University,undefined
[9] Photosynthesis Research Center,undefined
[10] Key Laboratory of Photobiology,undefined
[11] Institute of Botany,undefined
[12] Chinese Academy of Sciences,undefined
[13] Leibniz-Institute DSMZ-German Collection of Microorganisms and Cell Cultures,undefined
[14] Braunschweig University of Technology,undefined
[15] Southern Illinois University,undefined
来源
Nature Communications | / 11卷
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摘要
The light-harvesting-reaction center complex (LH1-RC) from the purple phototrophic bacterium Thiorhodovibrio strain 970 exhibits an LH1 absorption maximum at 960 nm, the most red-shifted absorption for any bacteriochlorophyll (BChl) a-containing species. Here we present a cryo-EM structure of the strain 970 LH1-RC complex at 2.82 Å resolution. The LH1 forms a closed ring structure composed of sixteen pairs of the αβ-polypeptides. Sixteen Ca ions are present in the LH1 C-terminal domain and are coordinated by residues from the αβ-polypeptides that are hydrogen-bonded to BChl a. The Ca2+-facilitated hydrogen-bonding network forms the structural basis of the unusual LH1 redshift. The structure also revealed the arrangement of multiple forms of α- and β-polypeptides in an individual LH1 ring. Such organization indicates a mechanism of interplay between the expression and assembly of the LH1 complex that is regulated through interactions with the RC subunits inside.
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