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

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 and Zheng-Yu Wang-Otomo ()
Additional contact information
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
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

Nature Communications, 2020, vol. 11, issue 1, 1-9

Abstract: 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.

Date: 2020
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DOI: 10.1038/s41467-020-18748-3

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