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Structural basis of outer membrane protein insertion by the BAM complex

Author

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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
    Jiangsu Province Key Laboratory of Anesthesiology, Xuzhou Medical College
    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)

  • 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)

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.

Suggested Citation

  • Yinghong Gu & Huanyu Li & Haohao Dong & Yi Zeng & Zhengyu Zhang & Neil G. Paterson & Phillip J. Stansfeld & Zhongshan Wang & Yizheng Zhang & Wenjian Wang & Changjiang Dong, 2016. "Structural basis of outer membrane protein insertion by the BAM complex," Nature, Nature, vol. 531(7592), pages 64-69, March.
    • Handle: RePEc:nat:nature:v:531:y:2016:i:7592:d:10.1038_nature17199
    DOI: 10.1038/nature17199
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    Cited by:

    1. Runrun Wu & Jeremy W. Bakelar & Karl Lundquist & Zijian Zhang & Katie M. Kuo & David Ryoo & Yui Tik Pang & Chen Sun & Tommi White & Thomas Klose & Wen Jiang & James C. Gumbart & Nicholas Noinaj, 2021. "Plasticity within the barrel domain of BamA mediates a hybrid-barrel mechanism by BAM," Nature Communications, Nature, vol. 12(1), pages 1-16, December.
    2. Parthasarathi Rath & Adrian Hermann & Ramona Schaefer & Elia Agustoni & Jean-Marie Vonach & Martin Siegrist & Christian Miscenic & Andreas Tschumi & Doris Roth & Christoph Bieniossek & Sebastian Hille, 2023. "High-throughput screening of BAM inhibitors in native membrane environment," Nature Communications, Nature, vol. 14(1), pages 1-11, December.

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