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Cryo-EM Structure of the Photosynthetic LH1-RC Complex from Rhodospirillum rubrum

K. Tani, R. Kanno, X.-C. Ji, M. Hall, L.-J. Yu, Y. Kimura, M. T. Madigan, A. Mizoguchi, B. M. Humbel, Z.-Y. Wang-Otomo
doi: https://doi.org/10.1101/2021.05.30.446358
K. Tani
1Graduate School of Medicine, Mie University, Tsu 514-8507, Japan
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  • For correspondence: ktani@doc.medic.mie-u.ac.jp wang@ml.ibaraki.ac.jp
R. Kanno
2Imaging Section, Research Support Division, Okinawa Institute of Science and Technology Graduate University (OIST), 1919-1, Tancha, Onna-son, Kunigami-gun, Okinawa 904-0495, Japan
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X.-C. Ji
3Faculty of Science, Ibaraki University, Mito 310-8512, Japan
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M. Hall
2Imaging Section, Research Support Division, Okinawa Institute of Science and Technology Graduate University (OIST), 1919-1, Tancha, Onna-son, Kunigami-gun, Okinawa 904-0495, Japan
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L.-J. Yu
4Photosynthesis Research Center, Key Laboratory of Photobiology, Institute of Botany, Chinese Academy of Sciences, Beijing 100093, China
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Y. Kimura
5Department of Agrobioscience, Graduate School of Agriculture, Kobe University, Nada, Kobe 657-8501, Japan
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M. T. Madigan
6School of Biological Sciences, Department of Microbiology, Southern Illinois University, Carbondale, IL 62901 USA
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A. Mizoguchi
1Graduate School of Medicine, Mie University, Tsu 514-8507, Japan
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B. M. Humbel
2Imaging Section, Research Support Division, Okinawa Institute of Science and Technology Graduate University (OIST), 1919-1, Tancha, Onna-son, Kunigami-gun, Okinawa 904-0495, Japan
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Z.-Y. Wang-Otomo
3Faculty of Science, Ibaraki University, Mito 310-8512, Japan
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  • For correspondence: ktani@doc.medic.mie-u.ac.jp wang@ml.ibaraki.ac.jp
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Abstract

We present a cryo-EM structure of the light-harvesting-reaction center (LH1-RC) core complex from purple phototrophic bacterium Rhodospirillum (Rsp.) rubrum at 2.76 Å resolution. The LH1 complex forms a closed, slightly elliptical ring structure with 16 αβ-polypeptides surrounding the RC. Our biochemical analysis detected rhodoquinone (RQ) molecules in the purified LH1-RC, and the cryo-EM density map specifically positions RQ at the QA site in the RC. The geranylgeraniol sidechains of bacteriochlorophyll (BChl) aG coordinated by LH1 β-polypeptides exhibit a highly homologous tail-up conformation that allows for interactions with the bacteriochlorin rings of nearby LH1 α-associated BChls aG. The structure also revealed key protein–protein interactions in both N- and C-terminal regions of the LH1 αβ-polypeptides, mainly within a face-to-face structural subunit. Our findings enable to evaluate past experimental and computational results obtained with this widely used organism and provide crucial information for more detailed exploration of light-energy conversion, quinone transport, and structure–function relationships in pigment-protein complexes.

Competing Interest Statement

The authors have declared no competing interest.

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Posted May 31, 2021.
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Cryo-EM Structure of the Photosynthetic LH1-RC Complex from Rhodospirillum rubrum
K. Tani, R. Kanno, X.-C. Ji, M. Hall, L.-J. Yu, Y. Kimura, M. T. Madigan, A. Mizoguchi, B. M. Humbel, Z.-Y. Wang-Otomo
bioRxiv 2021.05.30.446358; doi: https://doi.org/10.1101/2021.05.30.446358
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Cryo-EM Structure of the Photosynthetic LH1-RC Complex from Rhodospirillum rubrum
K. Tani, R. Kanno, X.-C. Ji, M. Hall, L.-J. Yu, Y. Kimura, M. T. Madigan, A. Mizoguchi, B. M. Humbel, Z.-Y. Wang-Otomo
bioRxiv 2021.05.30.446358; doi: https://doi.org/10.1101/2021.05.30.446358

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