The Library
Structural basis of outer membrane protein insertion by the BAM complex
Tools
Tools
Tools
Gu, Yinghong, Li, Huanyu, Dong, Haohao, Zeng, Yi, Zhang, Zhengyu, Paterson, Neil G., Stansfeld, Phillip J., Wang, Zhongshan, Zhang, Yizheng, Wang, Wenjian and Dong, Changjiang (2016) Structural basis of outer membrane protein insertion by the BAM complex. Nature, 531 (7592). pp. 64-69. doi:10.1038/nature17199 ISSN 0028-0836.
|
PDF
WRAP-structural-basis-outer-membrane-protein-insertion-complex-2016.pdf - Accepted Version - Requires a PDF viewer. Download (48Mb) | Preview |
Official URL: http://dx.doi.org/10.1038/nature17199
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.
| Item Type: | Journal Article | |||||||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
| Subjects: | Q Science > QH Natural history Q Science > QP Physiology Q Science > QR Microbiology |
|||||||||||||||
| Divisions: | Faculty of Science, Engineering and Medicine > Science > Life Sciences (2010- ) | |||||||||||||||
| Library of Congress Subject Headings (LCSH): | Gram-negative bacteria , Membrane proteins, Escherichia coli, Proteins, Cell membranes | |||||||||||||||
| Journal or Publication Title: | Nature | |||||||||||||||
| Publisher: | Nature Publishing | |||||||||||||||
| ISSN: | 0028-0836 | |||||||||||||||
| Official Date: | 3 March 2016 | |||||||||||||||
| Dates: |
|
|||||||||||||||
| Volume: | 531 | |||||||||||||||
| Number: | 7592 | |||||||||||||||
| Page Range: | pp. 64-69 | |||||||||||||||
| DOI: | 10.1038/nature17199 | |||||||||||||||
| Status: | Peer Reviewed | |||||||||||||||
| Publication Status: | Published | |||||||||||||||
| Access rights to Published version: | Restricted or Subscription Access | |||||||||||||||
| Date of first compliant deposit: | 11 November 2019 | |||||||||||||||
| Date of first compliant Open Access: | 11 November 2019 | |||||||||||||||
| RIOXX Funder/Project Grant: |
|
|||||||||||||||
| Related URLs: |
Request changes or add full text files to a record
Repository staff actions (login required)
 |
View Item |
Downloads
Downloads per month over past year
