Structural basis of outer membrane protein insertion by the BAM complex

Yinghong Gu, Huanyu Li, Haohao Dong, Yi Zeng, Zhengyu Zhang, Neil G. Paterson, Phillip J. Stansfeld, Zhongshan Wang, Yizheng Zhang, Wenjian Wang () and Changjiang Dong ()
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Yinghong Gu: Biomedical Research Centre, Norwich Medical School, University of East Anglia
Huanyu Li: Biomedical Research Centre, Norwich Medical School, University of East Anglia
Haohao Dong: Biomedical Research Centre, Norwich Medical School, University of East Anglia
Yi Zeng: Biomedical Research Centre, Norwich Medical School, University of East Anglia
Zhengyu Zhang: Biomedical Research Centre, Norwich Medical School, University of East Anglia
Neil G. Paterson: Diamond Light Source, Harwell Science and Innovation Campus
Phillip J. Stansfeld: University of Oxford
Zhongshan Wang: Biomedical Research Centre, Norwich Medical School, University of East Anglia
Yizheng Zhang: Key Laboratory of Bio-resources and Eco-environment, Ministry of Education, Sichuan Key Laboratory of Molecular Biology and Biotechnology, College of Life Sciences, Sichuan University
Wenjian Wang: the First Affiliated Hospital, Sun Yat-sen University
Changjiang Dong: Biomedical Research Centre, Norwich Medical School, University of East Anglia

Nature, 2016, vol. 531, issue 7592, 64-69

Abstract: Abstract 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.

Date: 2016
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DOI: 10.1038/nature17199

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