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

Author

Listed:
  • Kazutoshi Tani

    (Mie University)

  • Ryo Kanno

    (Imaging Section, Research Support Division, Okinawa Institute of Science and Technology Graduate University (OIST))

  • Yuki Makino

    (Faculty of Science, Ibaraki University)

  • Malgorzata Hall

    (Imaging Section, Research Support Division, Okinawa Institute of Science and Technology Graduate University (OIST))

  • Mizuki Takenouchi

    (Faculty of Science, Ibaraki University)

  • Michie Imanishi

    (Graduate School of Agriculture, Kobe University)

  • Long-Jiang Yu

    (Photosynthesis Research Center, Key Laboratory of Photobiology, Institute of Botany, Chinese Academy of Sciences)

  • Jörg Overmann

    (Leibniz-Institute DSMZ-German Collection of Microorganisms and Cell Cultures
    Braunschweig University of Technology)

  • Michael T. Madigan

    (Southern Illinois University)

  • Yukihiro Kimura

    (Graduate School of Agriculture, Kobe University)

  • Akira Mizoguchi

    (Mie University)

  • Bruno M. Humbel

    (Imaging Section, Research Support Division, Okinawa Institute of Science and Technology Graduate University (OIST))

  • Zheng-Yu Wang-Otomo

    (Faculty of Science, Ibaraki University)

Abstract

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.

Suggested Citation

  • 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. Hum, 2020. "Cryo-EM structure of a Ca2+-bound photosynthetic LH1-RC complex containing multiple αβ-polypeptides," Nature Communications, Nature, vol. 11(1), pages 1-9, December.
    • Handle: RePEc:nat:natcom:v:11:y:2020:i:1:d:10.1038_s41467-020-18748-3
    DOI: 10.1038/s41467-020-18748-3
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    Cited by:

    1. Kazutoshi Tani & Kenji V. P. Nagashima & Ryo Kanno & Saki Kawamura & Riku Kikuchi & Malgorzata Hall & Long-Jiang Yu & Yukihiro Kimura & Michael T. Madigan & Akira Mizoguchi & Bruno M. Humbel & Zheng-Y, 2021. "A previously unrecognized membrane protein in the Rhodobacter sphaeroides LH1-RC photocomplex," Nature Communications, Nature, vol. 12(1), pages 1-9, December.

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