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Cryo-EM structures of lipopolysaccharide transporter LptB2FGC in lipopolysaccharide or AMP-PNP-bound states reveal its transport mechanism

Author

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  • Xiaodi Tang

    (Sichuan University and Collaborative Innovation Center of Biotherapy)

  • Shenghai Chang

    (Zhejiang University School of Medicine
    Zhejiang University)

  • Qinghua Luo

    (Sichuan University and Collaborative Innovation Center of Biotherapy)

  • Zhengyu Zhang

    (Wuhan University)

  • Wen Qiao

    (Sichuan University and Collaborative Innovation Center of Biotherapy)

  • Caihuang Xu

    (Zhejiang University School of Medicine)

  • Changbin Zhang

    (Sichuan University and Collaborative Innovation Center of Biotherapy)

  • Yang Niu

    (Sichuan University and Collaborative Innovation Center of Biotherapy)

  • Wenxian Yang

    (Sichuan University and Collaborative Innovation Center of Biotherapy
    Sichuan University)

  • Ting Wang

    (Sichuan University and Collaborative Innovation Center of Biotherapy)

  • Zhibo Zhang

    (Sichuan University and Collaborative Innovation Center of Biotherapy)

  • Xiaofeng Zhu

    (Sichuan University and Collaborative Innovation Center of Biotherapy
    Sichuan University)

  • Xiawei Wei

    (Sichuan University and Collaborative Innovation Center of Biotherapy)

  • Changjiang Dong

    (Norwich Research Park)

  • Xing Zhang

    (Zhejiang University School of Medicine
    Zhejiang University)

  • Haohao Dong

    (Sichuan University and Collaborative Innovation Center of Biotherapy)

Abstract

Lipopolysaccharides (LPS) of Gram-negative bacteria are critical for the defence against cytotoxic substances and must be transported from the inner membrane (IM) to the outer membrane (OM) through a bridge formed by seven membrane proteins (LptBFGCADE). The IM component LptB2FG powers the process through a yet unclarified mechanism. Here we report three high-resolution cryo-EM structures of LptB2FG alone and complexed with LptC (LptB2FGC), trapped in either the LPS- or AMP-PNP-bound state. The structures reveal conformational changes between these states and substrate binding with or without LptC. We identify two functional transmembrane arginine-containing loops interacting with the bound AMP-PNP and elucidate allosteric communications between the domains. AMP-PNP binding induces an inward rotation and shift of the transmembrane helices of LptFG and LptC to tighten the cavity, with the closure of two lateral gates, to eventually expel LPS into the bridge. Functional assays reveal the functionality of the LptF and LptG periplasmic domains. Our findings shed light on the LPS transport mechanism.

Suggested Citation

  • Xiaodi Tang & Shenghai Chang & Qinghua Luo & Zhengyu Zhang & Wen Qiao & Caihuang Xu & Changbin Zhang & Yang Niu & Wenxian Yang & Ting Wang & Zhibo Zhang & Xiaofeng Zhu & Xiawei Wei & Changjiang Dong &, 2019. "Cryo-EM structures of lipopolysaccharide transporter LptB2FGC in lipopolysaccharide or AMP-PNP-bound states reveal its transport mechanism," Nature Communications, Nature, vol. 10(1), pages 1-12, December.
    • Handle: RePEc:nat:natcom:v:10:y:2019:i:1:d:10.1038_s41467-019-11977-1
    DOI: 10.1038/s41467-019-11977-1
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    Cited by:

    1. Jun Gyou Park & Songwon Kim & Eunhong Jang & Seung Hun Choi & Hyunsu Han & Seulgi Ju & Ji Won Kim & Da Sol Min & Mi Sun Jin, 2022. "The lysosomal transporter TAPL has a dual role as peptide translocator and phosphatidylserine floppase," Nature Communications, Nature, vol. 13(1), pages 1-16, December.
    2. Xing Chen & Chunyu Yu & Xinhua Liu & Beibei Liu & Xiaodi Wu & Jiajing Wu & Dong Yan & Lulu Han & Zifan Tang & Xinyi Yuan & Jianqiu Wang & Yue Wang & Shumeng Liu & Lin Shan & Yongfeng Shang, 2022. "Intracellular galectin-3 is a lipopolysaccharide sensor that promotes glycolysis through mTORC1 activation," Nature Communications, Nature, vol. 13(1), pages 1-18, December.
    3. Sille Remm & Dario Vecchis & Jendrik Schöppe & Cedric A. J. Hutter & Imre Gonda & Michael Hohl & Simon Newstead & Lars V. Schäfer & Markus A. Seeger, 2023. "Structural basis for triacylglyceride extraction from mycobacterial inner membrane by MFS transporter Rv1410," Nature Communications, Nature, vol. 14(1), pages 1-17, December.

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