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EMBO Rep. 2011 Feb;12(2):123-8. doi: 10.1038/embor.2010.202. Epub 2011 Jan 7.

Structure and function of BamE within the outer membrane and the β-barrel assembly machine.

Author information

1
School of Cancer Sciences, University of Birmingham, Edgbaston, Birmingham B15 2TT, UK.

Abstract

Insertion of folded proteins into the outer membrane of Gram-negative bacteria is mediated by the essential β-barrel assembly machine (Bam). Here, we report the native structure and mechanism of a core component of this complex, BamE, and show that it is exclusively monomeric in its native environment of the periplasm, but is able to adopt a distinct dimeric conformation in the cytoplasm. BamE is shown to bind specifically to phosphatidylglycerol, and comprehensive mutagenesis and interaction studies have mapped key determinants for complex binding, outer membrane integrity and cell viability, as well as revealing the role of BamE within the Bam complex.

PMID:
21212804
PMCID:
PMC3049429
DOI:
10.1038/embor.2010.202
[Indexed for MEDLINE]
Free PMC Article

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