IDEAS home Printed from https://ideas.repec.org/a/nat/nature/v534y2016i7605d10.1038_nature18020.html
   My bibliography  Save this article

Structure of spinach photosystem II–LHCII supercomplex at 3.2 Å resolution

Author

Listed:
  • Xuepeng Wei

    (National Laboratory of Biomacromolecules, CAS Center for Excellence in Biomacromolecules, Institute of Biophysics, Chinese Academy of Sciences
    University of Chinese Academy of Sciences)

  • Xiaodong Su

    (National Laboratory of Biomacromolecules, CAS Center for Excellence in Biomacromolecules, Institute of Biophysics, Chinese Academy of Sciences)

  • Peng Cao

    (National Laboratory of Biomacromolecules, CAS Center for Excellence in Biomacromolecules, Institute of Biophysics, Chinese Academy of Sciences)

  • Xiuying Liu

    (National Laboratory of Biomacromolecules, CAS Center for Excellence in Biomacromolecules, Institute of Biophysics, Chinese Academy of Sciences
    University of Chinese Academy of Sciences)

  • Wenrui Chang

    (National Laboratory of Biomacromolecules, CAS Center for Excellence in Biomacromolecules, Institute of Biophysics, Chinese Academy of Sciences)

  • Mei Li

    (National Laboratory of Biomacromolecules, CAS Center for Excellence in Biomacromolecules, Institute of Biophysics, Chinese Academy of Sciences)

  • Xinzheng Zhang

    (National Laboratory of Biomacromolecules, CAS Center for Excellence in Biomacromolecules, Institute of Biophysics, Chinese Academy of Sciences)

  • Zhenfeng Liu

    (National Laboratory of Biomacromolecules, CAS Center for Excellence in Biomacromolecules, Institute of Biophysics, Chinese Academy of Sciences)

Abstract

During photosynthesis, the plant photosystem II core complex receives excitation energy from the peripheral light-harvesting complex II (LHCII). The pathways along which excitation energy is transferred between them, and their assembly mechanisms, remain to be deciphered through high-resolution structural studies. Here we report the structure of a 1.1-megadalton spinach photosystem II–LHCII supercomplex solved at 3.2 Å resolution through single-particle cryo-electron microscopy. The structure reveals a homodimeric supramolecular system in which each monomer contains 25 protein subunits, 105 chlorophylls, 28 carotenoids and other cofactors. Three extrinsic subunits (PsbO, PsbP and PsbQ), which are essential for optimal oxygen-evolving activity of photosystem II, form a triangular crown that shields the Mn4CaO5-binding domains of CP43 and D1. One major trimeric and two minor monomeric LHCIIs associate with each core-complex monomer, and the antenna–core interactions are reinforced by three small intrinsic subunits (PsbW, PsbH and PsbZ). By analysing the closely connected interfacial chlorophylls, we have obtained detailed insights into the energy-transfer pathways between the antenna and core complexes.

Suggested Citation

  • Xuepeng Wei & Xiaodong Su & Peng Cao & Xiuying Liu & Wenrui Chang & Mei Li & Xinzheng Zhang & Zhenfeng Liu, 2016. "Structure of spinach photosystem II–LHCII supercomplex at 3.2 Å resolution," Nature, Nature, vol. 534(7605), pages 69-74, June.
  • Handle: RePEc:nat:nature:v:534:y:2016:i:7605:d:10.1038_nature18020
    DOI: 10.1038/nature18020
    as

    Download full text from publisher

    File URL: https://www.nature.com/articles/nature18020
    File Function: Abstract
    Download Restriction: Access to the full text of the articles in this series is restricted.

    File URL: https://libkey.io/10.1038/nature18020?utm_source=ideas
    LibKey link: if access is restricted and if your library uses this service, LibKey will redirect you to where you can use your library subscription to access this item
    ---><---

    As the access to this document is restricted, you may want to search for a different version of it.

    Citations

    Citations are extracted by the CitEc Project, subscribe to its RSS feed for this item.
    as


    Cited by:

    1. Hou, Jingxiang & Liu, Xuezhi & Zhang, Jiarui & Wei, Zhenhua & Ma, Yingying & Wan, Heng & Liu, Jie & Cui, Bingjing & Zong, Yuzheng & Chen, Yiting & Liang, Kehao & Liu, Fulai, 2023. "Combined application of biochar and partial root-zone drying irrigation improves water relations and water use efficiency of cotton plants under salt stress," Agricultural Water Management, Elsevier, vol. 290(C).
    2. Zhiyuan Mao & Xingyue Li & Zhenhua Li & Liangliang Shen & Xiaoyi Li & Yanyan Yang & Wenda Wang & Tingyun Kuang & Jian-Ren Shen & Guangye Han, 2024. "Structure and distinct supramolecular organization of a PSII-ACPII dimer from a cryptophyte alga Chroomonas placoidea," Nature Communications, Nature, vol. 15(1), pages 1-14, December.
    3. Yu-Zhong Zhang & Kang Li & Bing-Yue Qin & Jian-Ping Guo & Quan-Bao Zhang & Dian-Li Zhao & Xiu-Lan Chen & Jun Gao & Lu-Ning Liu & Long-Sheng Zhao, 2024. "Structure of cryptophyte photosystem II–light-harvesting antennae supercomplex," Nature Communications, Nature, vol. 15(1), pages 1-12, December.
    4. 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.
    5. Ryo Nagao & Koji Kato & Minoru Kumazawa & Kentaro Ifuku & Makio Yokono & Takehiro Suzuki & Naoshi Dohmae & Fusamichi Akita & Seiji Akimoto & Naoyuki Miyazaki & Jian-Ren Shen, 2022. "Structural basis for different types of hetero-tetrameric light-harvesting complexes in a diatom PSII-FCPII supercomplex," Nature Communications, Nature, vol. 13(1), pages 1-12, December.
    6. 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.

    More about this item

    Statistics

    Access and download statistics

    Corrections

    All material on this site has been provided by the respective publishers and authors. You can help correct errors and omissions. When requesting a correction, please mention this item's handle: RePEc:nat:nature:v:534:y:2016:i:7605:d:10.1038_nature18020. See general information about how to correct material in RePEc.

    If you have authored this item and are not yet registered with RePEc, we encourage you to do it here. This allows to link your profile to this item. It also allows you to accept potential citations to this item that we are uncertain about.

    We have no bibliographic references for this item. You can help adding them by using this form .

    If you know of missing items citing this one, you can help us creating those links by adding the relevant references in the same way as above, for each refering item. If you are a registered author of this item, you may also want to check the "citations" tab in your RePEc Author Service profile, as there may be some citations waiting for confirmation.

    For technical questions regarding this item, or to correct its authors, title, abstract, bibliographic or download information, contact: Sonal Shukla or Springer Nature Abstracting and Indexing (email available below). General contact details of provider: http://www.nature.com .

    Please note that corrections may take a couple of weeks to filter through the various RePEc services.

    IDEAS is a RePEc service. RePEc uses bibliographic data supplied by the respective publishers.