The structure of the β-barrel assembly machinery complex
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]
- 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:
- Grant/Contract Number:
- W-31-109-Eng-38; 1K22AI113078-01
- Type:
- Accepted Manuscript
- Journal Name:
- Science
- Additional Journal Information:
- Journal Volume: 351; Journal Issue: 6269; Journal ID: ISSN 0036-8075
- Publisher:
- AAAS
- 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 Orgs:
- National Inst. of Health (NIH), Bethesda, MD (United States)
- Country of Publication:
- United States
- Language:
- ENGLISH
- Subject:
- 59 BASIC BIOLOGICAL SCIENCES
- OSTI Identifier:
- 1252735
- Free Publicly Accessible Full Text
-
Accepted Manuscript (DOE)
- Publisher's Version of Record
- https://doi.org/10.1126/science.aad3460