Structural basis for bacterial lipoprotein relocation by the transporter LolCDE

Tang, Xiaodi, Chang, Shenghai, Zhang, Ke, Luo, Qinghua, Zhang, Zhengyu, Wang, Ting, Qiao, Wen, Wang, Chen, Shen, Chongrong, Zhang, Zhibo, Zhu, Xiaofeng, Wei, Xiawei, Dong, Changjiang, Zhang, Xing and Dong, Haohao (2021) Structural basis for bacterial lipoprotein relocation by the transporter LolCDE. Nature Structural & Molecular Biology, 28 (4). pp. 347-355. ISSN 1545-9993

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Abstract

Lipoproteins in the outer membrane of Gram-negative bacteria are involved in various vital physiological activities, including multidrug resistance. Synthesized in the cytoplasm and matured in the inner membrane, lipoproteins must be transported to the outer membrane through the Lol pathway mediated by the ATP-binding cassette transporter LolCDE in the inner membrane via an unknown mechanism. Here, we report cryo-EM structures of Escherichia coli LolCDE in apo, lipoprotein-bound, LolA-bound, ADP-bound and AMP-PNP-bound states at a resolution of 3.2–3.8 Å, covering the complete lipoprotein transport cycle. Mutagenesis and in vivo viability assays verify features of the structures and reveal functional residues and structural characteristics of LolCDE. The results provide insights into the mechanisms of sorting and transport of outer-membrane lipoproteins and may guide the development of novel therapies against multidrug-resistant Gram-negative bacteria.

Item Type:	Article
Faculty \ School:	Faculty of Medicine and Health Sciences > Norwich Medical School
Related URLs:	http://www.scopus.com/inward/record.url?... http://www.nature.com/articles/s41594-02...
Depositing User:	LivePure Connector
Date Deposited:	30 May 2021 00:01
Last Modified:	08 Mar 2024 11:33
URI:	https://ueaeprints.uea.ac.uk/id/eprint/80175
DOI:	10.1038/s41594-021-00573-x

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