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Crystal structure of spinach major light-harvesting complex at 2.72 Å resolution

Author

Listed:
  • Zhenfeng Liu

    (Institute of Biophysics, Chinese Academy of Sciences)

  • Hanchi Yan

    (Institute of Biophysics, Chinese Academy of Sciences)

  • Kebin Wang

    (Institute of Botany, Chinese Academy of Sciences)

  • Tingyun Kuang

    (Institute of Botany, Chinese Academy of Sciences)

  • Jiping Zhang

    (Institute of Biophysics, Chinese Academy of Sciences)

  • Lulu Gui

    (Institute of Biophysics, Chinese Academy of Sciences)

  • Xiaomin An

    (Institute of Biophysics, Chinese Academy of Sciences)

  • Wenrui Chang

    (Institute of Biophysics, Chinese Academy of Sciences)

Abstract

The major light-harvesting complex of photosystem II (LHC-II) serves as the principal solar energy collector in the photosynthesis of green plants and presumably also functions in photoprotection under high-light conditions. Here we report the first X-ray structure of LHC-II in icosahedral proteoliposome assembly at atomic detail. One asymmetric unit of a large R32 unit cell contains ten LHC-II monomers. The 14 chlorophylls (Chl) in each monomer can be unambiguously distinguished as eight Chla and six Chlb molecules. Assignment of the orientation of the transition dipole moment of each chlorophyll has been achieved. All Chlb are located around the interface between adjacent monomers, and together with Chla they are the basis for efficient light harvesting. Four carotenoid-binding sites per monomer have been observed. The xanthophyll-cycle carotenoid at the monomer–monomer interface may be involved in the non-radiative dissipation of excessive energy, one of the photoprotective strategies that have evolved in plants.

Suggested Citation

  • Zhenfeng Liu & Hanchi Yan & Kebin Wang & Tingyun Kuang & Jiping Zhang & Lulu Gui & Xiaomin An & Wenrui Chang, 2004. "Crystal structure of spinach major light-harvesting complex at 2.72 Å resolution," Nature, Nature, vol. 428(6980), pages 287-292, March.
    • Handle: RePEc:nat:nature:v:428:y:2004:i:6980:d:10.1038_nature02373
    DOI: 10.1038/nature02373
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    Cited by:

    1. Wu, Wenbo & Tan, Ling & Chang, Haixing & Zhang, Chaofan & Tan, Xuefei & Liao, Qiang & Zhong, Nianbing & Zhang, Xianming & Zhang, Yuanbo & Ho, Shih-Hsin, 2023. "Advancements on process regulation for microalgae-based carbon neutrality and biodiesel production," Renewable and Sustainable Energy Reviews, Elsevier, vol. 171(C).
    2. Makiko Kosugi & Masato Kawasaki & Yutaka Shibata & Kojiro Hara & Shinichi Takaichi & Toshio Moriya & Naruhiko Adachi & Yasuhiro Kamei & Yasuhiro Kashino & Sakae Kudoh & Hiroyuki Koike & Toshiya Senda, 2023. "Uphill energy transfer mechanism for photosynthesis in an Antarctic alga," Nature Communications, Nature, vol. 14(1), pages 1-14, December.
    3. Mengyuan Zheng & Xiaojie Pang & Ming Chen & Lijin Tian, 2024. "Ultrafast energy quenching mechanism of LHCSR3-dependent photoprotection in Chlamydomonas," Nature Communications, Nature, vol. 15(1), pages 1-10, December.
    4. Songhao Zhao & Lili Shen & Xiaoyi Li & Qiushuang Tao & Zhenhua Li & Caizhe Xu & Cuicui Zhou & Yanyan Yang & Min Sang & Guangye Han & Long-Jiang Yu & Tingyun Kuang & Jian-Ren Shen & Wenda Wang, 2023. "Structural insights into photosystem II supercomplex and trimeric FCP antennae of a centric diatom Cyclotella meneghiniana," Nature Communications, Nature, vol. 14(1), pages 1-15, December.
    5. Long Si & Shumeng Zhang & Xiaodong Su & Mei Li, 2024. "Structural basis for the distinct core-antenna assembly of cryptophyte photosystem II," Nature Communications, Nature, vol. 15(1), pages 1-15, December.

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