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Cryo-EM structure of the RC-LH core complex from an early branching photosynthetic prokaryote

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  • Yueyong Xin

    (Hangzhou Normal University)

  • Yang Shi

    (Chinese Academy of Sciences
    University of Chinese Academy of Sciences)

  • Tongxin Niu

    (Chinese Academy of Sciences
    University of Chinese Academy of Sciences)

  • Qingqiang Wang

    (Hangzhou Normal University)

  • Wanqiang Niu

    (Hangzhou Normal University)

  • Xiaojun Huang

    (Chinese Academy of Sciences)

  • Wei Ding

    (Chinese Academy of Sciences)

  • Lei Yang

    (Hangzhou Normal University)

  • Robert E. Blankenship

    (Washington University in St. Louis)

  • Xiaoling Xu

    (Hangzhou Normal University)

  • Fei Sun

    (Chinese Academy of Sciences
    University of Chinese Academy of Sciences
    Chinese Academy of Sciences)

Abstract

Photosynthetic prokaryotes evolved diverse light-harvesting (LH) antennas to absorb sunlight and transfer energy to reaction centers (RC). The filamentous anoxygenic phototrophs (FAPs) are important early branching photosynthetic bacteria in understanding the origin and evolution of photosynthesis. How their photosynthetic machinery assembles for efficient energy transfer is yet to be elucidated. Here, we report the 4.1 Å structure of photosynthetic core complex from Roseiflexus castenholzii by cryo-electron microscopy. The RC–LH complex has a tetra-heme cytochrome c bound RC encompassed by an elliptical LH ring that is assembled from 15 LHαβ subunits. An N-terminal transmembrane helix of cytochrome c inserts into the LH ring, not only yielding a tightly bound cytochrome c for rapid electron transfer, but also opening a slit in the LH ring, which is further flanked by a transmembrane helix from a newly discovered subunit X. These structural features suggest an unusual quinone exchange model of prokaryotic photosynthetic machinery.

Suggested Citation

  • Yueyong Xin & Yang Shi & Tongxin Niu & Qingqiang Wang & Wanqiang Niu & Xiaojun Huang & Wei Ding & Lei Yang & Robert E. Blankenship & Xiaoling Xu & Fei Sun, 2018. "Cryo-EM structure of the RC-LH core complex from an early branching photosynthetic prokaryote," Nature Communications, Nature, vol. 9(1), pages 1-10, December.
    • Handle: RePEc:nat:natcom:v:9:y:2018:i:1:d:10.1038_s41467-018-03881-x
    DOI: 10.1038/s41467-018-03881-x
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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.
    2. Shishang Dong & Guoqiang Huang & Changhui Wang & Jiajia Wang & Sen-Fang Sui & Xiaochun Qin, 2022. "Structure of the Acidobacteria homodimeric reaction center bound with cytochrome c," Nature Communications, Nature, vol. 13(1), pages 1-13, December.
    3. Peng Cao & Laura Bracun & Atsushi Yamagata & Bern M. Christianson & Tatsuki Negami & Baohua Zou & Tohru Terada & Daniel P. Canniffe & Mikako Shirouzu & Mei Li & Lu-Ning Liu, 2022. "Structural basis for the assembly and quinone transport mechanisms of the dimeric photosynthetic RC–LH1 supercomplex," Nature Communications, Nature, vol. 13(1), pages 1-12, December.

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