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

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 (), Xing Zhang () and Haohao Dong ()
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Xiaodi Tang: Sichuan University and Collaborative Innovation Center of Biotherapy
Shenghai Chang: Zhejiang University School of Medicine
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
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
Xiawei Wei: Sichuan University and Collaborative Innovation Center of Biotherapy
Changjiang Dong: Norwich Research Park
Xing Zhang: Zhejiang University School of Medicine
Haohao Dong: Sichuan University and Collaborative Innovation Center of Biotherapy

Nature Communications, 2019, vol. 10, issue 1, 1-12

Abstract: 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.

Date: 2019
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DOI: 10.1038/s41467-019-11977-1

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