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Structural basis for directional chitin biosynthesis

Author

Listed:
  • Wei Chen

    (Chinese Academy of Agricultural Sciences
    Chinese Academy of Agricultural Sciences)

  • Peng Cao

    (Beijing University of Technology)

  • Yuansheng Liu

    (Dalian University of Technology)

  • Ailing Yu

    (Chinese Academy of Agricultural Sciences)

  • Dong Wang

    (Dalian University of Technology)

  • Lei Chen

    (Chinese Academy of Agricultural Sciences)

  • Rajamanikandan Sundarraj

    (Tianjin University)

  • Zhiguang Yuchi

    (Tianjin University)

  • Yong Gong

    (Chinese Academy of Sciences)

  • Hans Merzendorfer

    (University of Siegen)

  • Qing Yang

    (Chinese Academy of Agricultural Sciences
    Chinese Academy of Agricultural Sciences
    Dalian University of Technology)

Abstract

Chitin, the most abundant aminopolysaccharide in nature, is an extracellular polymer consisting of N-acetylglucosamine (GlcNAc) units1. The key reactions of chitin biosynthesis are catalysed by chitin synthase2–4, a membrane-integrated glycosyltransferase that transfers GlcNAc from UDP-GlcNAc to a growing chitin chain. However, the precise mechanism of this process has yet to be elucidated. Here we report five cryo-electron microscopy structures of a chitin synthase from the devastating soybean root rot pathogenic oomycete Phytophthora sojae (PsChs1). They represent the apo, GlcNAc-bound, nascent chitin oligomer-bound, UDP-bound (post-synthesis) and chitin synthase inhibitor nikkomycin Z-bound states of the enzyme, providing detailed views into the multiple steps of chitin biosynthesis and its competitive inhibition. The structures reveal the chitin synthesis reaction chamber that has the substrate-binding site, the catalytic centre and the entrance to the polymer-translocating channel that allows the product polymer to be discharged. This arrangement reflects consecutive key events in chitin biosynthesis from UDP-GlcNAc binding and polymer elongation to the release of the product. We identified a swinging loop within the chitin-translocating channel, which acts as a ‘gate lock’ that prevents the substrate from leaving while directing the product polymer into the translocating channel for discharge to the extracellular side of the cell membrane. This work reveals the directional multistep mechanism of chitin biosynthesis and provides a structural basis for inhibition of chitin synthesis.

Suggested Citation

  • Wei Chen & Peng Cao & Yuansheng Liu & Ailing Yu & Dong Wang & Lei Chen & Rajamanikandan Sundarraj & Zhiguang Yuchi & Yong Gong & Hans Merzendorfer & Qing Yang, 2022. "Structural basis for directional chitin biosynthesis," Nature, Nature, vol. 610(7931), pages 402-408, October.
  • Handle: RePEc:nat:nature:v:610:y:2022:i:7931:d:10.1038_s41586-022-05244-5
    DOI: 10.1038/s41586-022-05244-5
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    Citations

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    Cited by:

    1. Dan-Dan Chen & Zhao-Bin Wang & Le-Xuan Wang & Peng Zhao & Cai-Hong Yun & Lin Bai, 2023. "Structure, catalysis, chitin transport, and selective inhibition of chitin synthase," Nature Communications, Nature, vol. 14(1), pages 1-13, December.
    2. Kyojiro N. Ikeda & Ilya Belevich & Luis Zelaya-Lainez & Lukas Orel & Josef Füssl & Jaromír Gumulec & Christian Hellmich & Eija Jokitalo & Florian Raible, 2024. "Dynamic microvilli sculpt bristles at nanometric scale," Nature Communications, Nature, vol. 15(1), pages 1-9, December.
    3. Jaroslaw Sedzicki & Dongchun Ni & Frank Lehmann & Henning Stahlberg & Christoph Dehio, 2024. "Structure-function analysis of the cyclic β-1,2-glucan synthase from Agrobacterium tumefaciens," Nature Communications, Nature, vol. 15(1), pages 1-10, December.

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