| Literature DB >> 27862971 |
Jeremy Bakelar1, Susan K Buchanan2, Nicholas Noinaj1.
Abstract
The β-barrel assembly machinery (BAM) is a multicomponent complex responsible for the biogenesis of β-barrel outer membrane proteins (OMPs) in Gram-negative bacteria, with conserved systems in both mitochondria and chloroplasts. Given its importance in the integrity of the outer membrane and in the assembly of surface exposed virulence factors, BAM is an attractive therapeutic target against pathogenic bacteria, particularly multidrug-resistant strains. While the mechanism for how BAM functions remains elusive, previous structural studies have described each of the individual components of BAM, offering only a few clues to how the complex functions. Recently, a number of structures have been reported of complexes, including that of fully assembled BAM in differing conformational states. These studies have provided the molecular blueprint detailing the atomic interactions between the components and have revealed new details about BAM, which suggest a dynamic mechanism that may use conformational changes to assist in the biogenesis of new OMPs. © Published 2016. This article is a U.S. Government work and is in the public domain in the USA.Entities:
Keywords: BAM complex; MD simulations; X-ray crystallography; lateral gate; membrane biogenesis; membrane protein; outer membrane protein; protein folding; β-barrel assembly machinery; β-barrel membrane proteins
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Year: 2016 PMID: 27862971 PMCID: PMC5429997 DOI: 10.1111/febs.13960
Source DB: PubMed Journal: FEBS J ISSN: 1742-464X Impact factor: 5.542