Structural basis of outer membrane protein insertion by the BAM complex

Gu, Yinghong, Li, Huanyu, Dong, Haohao, Zeng, Yi, Zhang, Zhengyu, Paterson, Neil G., Stansfeld, Phillip J, Wang, Zhongshan, Zhang, Yizheng, Wang, Wenjian and Dong, Changjiang (2016) Structural basis of outer membrane protein insertion by the BAM complex. Nature, 531. 64–69. ISSN 0028-0836

[thumbnail of BAM_Nature_Gu_29012016_2_change_Figure_legends_3_revised_accepted]
PDF (BAM_Nature_Gu_29012016_2_change_Figure_legends_3_revised_accepted) - Accepted Version
Download (49MB) | Preview


All Gram-negative bacteria, mitochondria and chloroplasts have outer membrane proteins (OMPs) that perform many fundamental biological processes. The OMPs in Gram-negative bacteria are inserted and folded into the outer membrane by the β-barrel assembly machinery (BAM). The mechanism involved is poorly understood, owing to the absence of a structure of the entire BAM complex. Here we report two crystal structures of the Escherichia coli BAM complex in two distinct states: an inward-open state and a lateral-open state. Our structures reveal that the five polypeptide transport-associated domains of BamA form a ring architecture with four associated lipoproteins, BamB–BamE, in the periplasm. Our structural, functional studies and molecular dynamics simulations indicate that these subunits rotate with respect to the integral membrane β-barrel of BamA to induce movement of the β-strands of the barrel and promote insertion of the nascent OMP.

Item Type: Article
Uncontrolled Keywords: x-ray crystallography,bacterial structural biology,membrane structure and assembly
Faculty \ School: Faculty of Medicine and Health Sciences > Norwich Medical School
UEA Research Groups: Faculty of Medicine and Health Sciences > Research Groups > Gastroenterology and Gut Biology
Depositing User: Pure Connector
Date Deposited: 18 Mar 2016 14:00
Last Modified: 21 Aug 2023 01:00
DOI: 10.1038/nature17199

Actions (login required)

View Item View Item