The structure of the β-barrel assembly machinery complex

doi:10.1126/science.aad3460

Title: The structure of the β-barrel assembly machinery complex

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Abstract

β-Barrel outer membrane proteins (OMPs) are found in the outer membranes of Gram-negative bacteria and are essential for nutrient import, signaling, and adhesion. A 200-kilodalton five-component complex called the β-barrel assembly machinery (BAM) complex has been implicated in the biogenesis of OMPs. In this paper, we report the structure of the BAM complex from Escherichia coli, revealing that binding of BamCDE modulates the conformation of BamA, the central component, which may serve to regulate the BAM complex. The periplasmic domain of BamA was in a closed state that prevents access to the barrel lumen, which indicates substrate OMPs may not be threaded through the barrel during biogenesis. Finally and further, conformational shifts in the barrel domain lead to opening of the exit pore and rearrangement at the lateral gate.

Authors:

Bakelar, Jeremy ^[1]; Buchanan, Susan K. ^[2]; Noinaj, Nicholas ^[1]

Purdue Univ., West Lafayette, IN (United States). Dept. of Biological Sciences. Markey Center for Structural Biology
National Inst. of Health (NIH), Bethesda, MD (United States). National Inst. of Diabetes and Digestive and Kidney Diseases

Publication Date:: 2016-01-08

Research Org.:: Purdue Univ., West Lafayette, IN (United States)

Sponsoring Org.:: USDOE Office of Science (SC), Basic Energy Sciences (BES) (SC-22); National Inst. of Health (NIH) (United States)

Contributing Org.:: National Inst. of Health (NIH), Bethesda, MD (United States)

OSTI Identifier:: 1252735

Grant/Contract Number:: W-31-109-Eng-38; 1K22AI113078-01

Resource Type:: Accepted Manuscript

Journal Name:: Science

Additional Journal Information:: Journal Volume: 351; Journal Issue: 6269; Journal ID: ISSN 0036-8075

Publisher:: AAAS

Country of Publication:: United States

Language:: ENGLISH

Subject:: 59 BASIC BIOLOGICAL SCIENCES

Citation Formats


                    Bakelar, Jeremy, Buchanan, Susan K., and Noinaj, Nicholas. The structure of the β-barrel assembly machinery complex.  United States: N. p., 2016. 
        Web.  doi:10.1126/science.aad3460.

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                    Bakelar, Jeremy, Buchanan, Susan K., & Noinaj, Nicholas. The structure of the β-barrel assembly machinery complex.  United States.  doi:10.1126/science.aad3460.

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                    Bakelar, Jeremy, Buchanan, Susan K., and Noinaj, Nicholas. Fri .  
        "The structure of the β-barrel assembly machinery complex".  United States.  doi:10.1126/science.aad3460.  https://www.osti.gov/servlets/purl/1252735.

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@article{osti_1252735,

  title        = {The structure of the β-barrel assembly machinery complex},

  author       = {Bakelar, Jeremy and Buchanan, Susan K. and Noinaj, Nicholas},

  abstractNote = {β-Barrel outer membrane proteins (OMPs) are found in the outer membranes of Gram-negative bacteria and are essential for nutrient import, signaling, and adhesion. A 200-kilodalton five-component complex called the β-barrel assembly machinery (BAM) complex has been implicated in the biogenesis of OMPs. In this paper, we report the structure of the BAM complex from Escherichia coli, revealing that binding of BamCDE modulates the conformation of BamA, the central component, which may serve to regulate the BAM complex. The periplasmic domain of BamA was in a closed state that prevents access to the barrel lumen, which indicates substrate OMPs may not be threaded through the barrel during biogenesis. Finally and further, conformational shifts in the barrel domain lead to opening of the exit pore and rearrangement at the lateral gate.},

  doi          = {10.1126/science.aad3460},

  journal      = {Science},

  number       = 6269,

  volume       = 351,

  place        = {United States},

  year         = {2016},

  month        = {1}

}

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DOI: 10.1126/science.aad3460

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