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

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:
 [1];  [2];  [1]
  1. Purdue Univ., West Lafayette, IN (United States). Dept. of Biological Sciences. Markey Center for Structural Biology
  2. National Inst. of Health (NIH), Bethesda, MD (United States). National Inst. of Diabetes and Digestive and Kidney Diseases
Publication Date:
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.
Bakelar, Jeremy, Buchanan, Susan K., & Noinaj, Nicholas. The structure of the β-barrel assembly machinery complex. United States. doi:10.1126/science.aad3460.
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.
@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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Cited by: 53 works
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