期刊
NATURE REVIEWS MICROBIOLOGY
卷 15, 期 4, 页码 -出版社
NATURE PUBLISHING GROUP
DOI: 10.1038/nrmicro.2016.191
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资金
- Department of Biological Sciences at Purdue University, Indiana, USA
- Showalter Trust Award
- US National Institute of Allergy and Infectious Diseases [1K22AI113078-01]
- US National Science Foundation [MCB-1452464]
- Intramural Research Program of the US National Institute of Diabetes and Digestive and Kidney Diseases, US National Institutes of Health
- Division Of Physics
- Direct For Mathematical & Physical Scien [1205878] Funding Source: National Science Foundation
- Div Of Molecular and Cellular Bioscience
- Direct For Biological Sciences [1452464] Funding Source: National Science Foundation
In Gram-negative bacteria, the biogenesis of beta -barrel outer membrane proteins (OMPs) is mediated by the beta-barrel assembly machinery (BAM) complex. During the past decade, structural and functional studies have collectively contributed to advancing our understanding of the structure and function of the BAM complex; however, the exact mechanism that is involved remains elusive. In this Progress article, we discuss recent structural studies that have revealed that the accessory proteins may regulate essential unprecedented conformational changes in the core component BamA during function. We also detail the mechanistic insights that have been gained from structural data, mutagenesis studies and molecular dynamics simulations, and explore two emerging models for the BAM-mediated biogenesis of OMPs in bacteria.
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