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

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

Seven lipopolysaccharide (LPS) transport proteins (LptBFGCADE) mediate the transport of LPS from the inner to the outer membrane of Gram-negative bacteria. Here the authors provide mechanistic insights into LPS recognition and transportation by determining the cryo-EM structures of the inner membran...

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Autores principales: 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, Haohao Dong
Formato: article
Lenguaje:EN
Publicado: Nature Portfolio 2019
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Acceso en línea:https://doaj.org/article/b2966fc978dc4035a64b64637481ce2f
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spelling oai:doaj.org-article:b2966fc978dc4035a64b64637481ce2f2021-12-02T14:35:31ZCryo-EM structures of lipopolysaccharide transporter LptB2FGC in lipopolysaccharide or AMP-PNP-bound states reveal its transport mechanism10.1038/s41467-019-11977-12041-1723https://doaj.org/article/b2966fc978dc4035a64b64637481ce2f2019-09-01T00:00:00Zhttps://doi.org/10.1038/s41467-019-11977-1https://doaj.org/toc/2041-1723Seven lipopolysaccharide (LPS) transport proteins (LptBFGCADE) mediate the transport of LPS from the inner to the outer membrane of Gram-negative bacteria. Here the authors provide mechanistic insights into LPS recognition and transportation by determining the cryo-EM structures of the inner membrane complex LptB2FGC bound to either LPS or AMP-PNP.Xiaodi TangShenghai ChangQinghua LuoZhengyu ZhangWen QiaoCaihuang XuChangbin ZhangYang NiuWenxian YangTing WangZhibo ZhangXiaofeng ZhuXiawei WeiChangjiang DongXing ZhangHaohao DongNature PortfolioarticleScienceQENNature Communications, Vol 10, Iss 1, Pp 1-12 (2019)
institution DOAJ
collection DOAJ
language EN
topic Science
Q
spellingShingle Science
Q
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
Haohao Dong
Cryo-EM structures of lipopolysaccharide transporter LptB2FGC in lipopolysaccharide or AMP-PNP-bound states reveal its transport mechanism
description Seven lipopolysaccharide (LPS) transport proteins (LptBFGCADE) mediate the transport of LPS from the inner to the outer membrane of Gram-negative bacteria. Here the authors provide mechanistic insights into LPS recognition and transportation by determining the cryo-EM structures of the inner membrane complex LptB2FGC bound to either LPS or AMP-PNP.
format article
author 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
Haohao Dong
author_facet 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
Haohao Dong
author_sort Xiaodi Tang
title Cryo-EM structures of lipopolysaccharide transporter LptB2FGC in lipopolysaccharide or AMP-PNP-bound states reveal its transport mechanism
title_short Cryo-EM structures of lipopolysaccharide transporter LptB2FGC in lipopolysaccharide or AMP-PNP-bound states reveal its transport mechanism
title_full Cryo-EM structures of lipopolysaccharide transporter LptB2FGC in lipopolysaccharide or AMP-PNP-bound states reveal its transport mechanism
title_fullStr Cryo-EM structures of lipopolysaccharide transporter LptB2FGC in lipopolysaccharide or AMP-PNP-bound states reveal its transport mechanism
title_full_unstemmed Cryo-EM structures of lipopolysaccharide transporter LptB2FGC in lipopolysaccharide or AMP-PNP-bound states reveal its transport mechanism
title_sort cryo-em structures of lipopolysaccharide transporter lptb2fgc in lipopolysaccharide or amp-pnp-bound states reveal its transport mechanism
publisher Nature Portfolio
publishDate 2019
url https://doaj.org/article/b2966fc978dc4035a64b64637481ce2f
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