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

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Structure and function of BamE within the outer membrane and the beta-barrel assembly machine. / Knowles, Timothy; Browning, Douglas; Jeeves, Mark; Maderbocus, Riyaz; Rajesh, Sandya; Sridhar, Pooja; Manoli, E; Emery, D; Sommer, Ulf; Spencer, A; Leyton, Denisse; Squire, D; Chaudhuri, RR; Viant, Mark; Cunningham, Adam; Henderson, Ian; Overduin, Michael.

In: EMBO Reports, Vol. 12, No. 2, 01.02.2011, p. 123-128.

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@article{9e6f739d89f74211bb32150d05e59690,
title = "Structure and function of BamE within the outer membrane and the beta-barrel assembly machine",
abstract = "Insertion of folded proteins into the outer membrane of Gram-negative bacteria is mediated by the essential beta-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.",
keywords = "Bam complex, Omp85, SmpA, outer membrane biogenesis, BamE",
author = "Timothy Knowles and Douglas Browning and Mark Jeeves and Riyaz Maderbocus and Sandya Rajesh and Pooja Sridhar and E Manoli and D Emery and Ulf Sommer and A Spencer and Denisse Leyton and D Squire and RR Chaudhuri and Mark Viant and Adam Cunningham and Ian Henderson and Michael Overduin",
year = "2011",
month = feb
day = "1",
doi = "10.1038/embor.2010.202",
language = "English",
volume = "12",
pages = "123--128",
journal = "EMBO Reports",
issn = "1469-221X",
publisher = "EMBO Press",
number = "2",

}

RIS

TY - JOUR

T1 - Structure and function of BamE within the outer membrane and the beta-barrel assembly machine

AU - Knowles, Timothy

AU - Browning, Douglas

AU - Jeeves, Mark

AU - Maderbocus, Riyaz

AU - Rajesh, Sandya

AU - Sridhar, Pooja

AU - Manoli, E

AU - Emery, D

AU - Sommer, Ulf

AU - Spencer, A

AU - Leyton, Denisse

AU - Squire, D

AU - Chaudhuri, RR

AU - Viant, Mark

AU - Cunningham, Adam

AU - Henderson, Ian

AU - Overduin, Michael

PY - 2011/2/1

Y1 - 2011/2/1

N2 - Insertion of folded proteins into the outer membrane of Gram-negative bacteria is mediated by the essential beta-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.

AB - Insertion of folded proteins into the outer membrane of Gram-negative bacteria is mediated by the essential beta-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.

KW - Bam complex

KW - Omp85

KW - SmpA

KW - outer membrane biogenesis

KW - BamE

U2 - 10.1038/embor.2010.202

DO - 10.1038/embor.2010.202

M3 - Article

C2 - 21212804

VL - 12

SP - 123

EP - 128

JO - EMBO Reports

JF - EMBO Reports

SN - 1469-221X

IS - 2

ER -