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Cryo-EM structure of the Blastochloris viridis LH1–RC complex at 2.9 Å

Author

Listed:
  • Pu Qian

    (University of Sheffield)

  • C. Alistair Siebert

    (Diamond Light Source)

  • Peiyi Wang

    (University of Leeds)

  • Daniel P. Canniffe

    (University of Sheffield)

  • C. Neil Hunter

    (University of Sheffield)

Abstract

The light-harvesting 1–reaction centre (LH1–RC) complex is a key functional component of bacterial photosynthesis. Here we present a 2.9 Å resolution cryo-electron microscopy structure of the bacteriochlorophyll b-based LH1–RC complex from Blastochloris viridis that reveals the structural basis for absorption of infrared light and the molecular mechanism of quinone migration across the LH1 complex. The triple-ring LH1 complex comprises a circular array of 17 β-polypeptides sandwiched between 17 α- and 16 γ-polypeptides. Tight packing of the γ-apoproteins between β-polypeptides collectively interlocks and stabilizes the LH1 structure; this, together with the short Mg–Mg distances of bacteriochlorophyll b pairs, contributes to the large redshift of bacteriochlorophyll b absorption. The ‘missing’ 17th γ-polypeptide creates a pore in the LH1 ring, and an adjacent binding pocket provides a folding template for a quinone, Q P, which adopts a compact, export-ready conformation before passage through the pore and eventual diffusion to the cytochrome bc 1 complex.

Suggested Citation

  • Pu Qian & C. Alistair Siebert & Peiyi Wang & Daniel P. Canniffe & C. Neil Hunter, 2018. "Cryo-EM structure of the Blastochloris viridis LH1–RC complex at 2.9 Å," Nature, Nature, vol. 556(7700), pages 203-208, April.
    • Handle: RePEc:nat:nature:v:556:y:2018:i:7700:d:10.1038_s41586-018-0014-5
    DOI: 10.1038/s41586-018-0014-5
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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. 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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