Studying assembly of the BAM complex in native membranes by cellular solid-state NMR spectroscopy

Cecilia de Agrela Pinto; Deni Mance; Manon Julien; Mark Daniels; Markus Weingarth; Marc Baldus

doi:10.1016/j.jsb.2017.11.015

Studying assembly of the BAM complex in native membranes by cellular solid-state NMR spectroscopy

Cecilia de Agrela Pinto, Deni Mance, Manon Julien, Mark Daniels, Markus Weingarth, Marc Baldus^*

^*Corresponding author for this work

Research output: Contribution to journal › Article › Academic › peer-review

Abstract

Significant progress has been made in obtaining structural insight into the assembly of the β-barrel assembly machinery complex (BAM). These crystallography and electron microscopy studies used detergent as a membrane mimetic and revealed structural variations in the central domain, BamA, as well as in the lipoprotein BamC. We have used cellular solid-state NMR spectroscopy to examine the entire BamABCDE complex in native outer membranes and obtained data on the BamCDE subcomplex in outer membranes, in addition to synthetic bilayers. To reduce spectral crowding, we utilized proton-detected experiments and employed amino-acid specific isotope-labelling in (13C, 13C) correlation experiments. Taken together, the results provide insight into the overall fold and assembly of the BAM complex in native membranes, in particular regarding the structural flexibility of BamC in the absence of the core unit BamA

Original language	English
Pages (from-to)	1-11
Journal	Journal of Structural Biology
Volume	206
Issue number	1
DOIs	https://doi.org/10.1016/j.jsb.2017.11.015
Publication status	Published - 1 Apr 2019

Keywords

Solid-state NMR
BAM
MAS
E. coli
Membrane protein complex

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10.1016/j.jsb.2017.11.015

1-s2.0-S1047847717302113-mainFinal published version, 5.35 MBLicence: Taverne

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title = "Studying assembly of the BAM complex in native membranes by cellular solid-state NMR spectroscopy",

abstract = "Significant progress has been made in obtaining structural insight into the assembly of the β-barrel assembly machinery complex (BAM). These crystallography and electron microscopy studies used detergent as a membrane mimetic and revealed structural variations in the central domain, BamA, as well as in the lipoprotein BamC. We have used cellular solid-state NMR spectroscopy to examine the entire BamABCDE complex in native outer membranes and obtained data on the BamCDE subcomplex in outer membranes, in addition to synthetic bilayers. To reduce spectral crowding, we utilized proton-detected experiments and employed amino-acid specific isotope-labelling in (13C, 13C) correlation experiments. Taken together, the results provide insight into the overall fold and assembly of the BAM complex in native membranes, in particular regarding the structural flexibility of BamC in the absence of the core unit BamA",

keywords = "Solid-state NMR, BAM, MAS, E. coli, Membrane protein complex",

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AU - de Agrela Pinto, Cecilia

AU - Mance, Deni

AU - Julien, Manon

AU - Daniels, Mark

AU - Weingarth, Markus

AU - Baldus, Marc

PY - 2019/4/1

Y1 - 2019/4/1

N2 - Significant progress has been made in obtaining structural insight into the assembly of the β-barrel assembly machinery complex (BAM). These crystallography and electron microscopy studies used detergent as a membrane mimetic and revealed structural variations in the central domain, BamA, as well as in the lipoprotein BamC. We have used cellular solid-state NMR spectroscopy to examine the entire BamABCDE complex in native outer membranes and obtained data on the BamCDE subcomplex in outer membranes, in addition to synthetic bilayers. To reduce spectral crowding, we utilized proton-detected experiments and employed amino-acid specific isotope-labelling in (13C, 13C) correlation experiments. Taken together, the results provide insight into the overall fold and assembly of the BAM complex in native membranes, in particular regarding the structural flexibility of BamC in the absence of the core unit BamA

AB - Significant progress has been made in obtaining structural insight into the assembly of the β-barrel assembly machinery complex (BAM). These crystallography and electron microscopy studies used detergent as a membrane mimetic and revealed structural variations in the central domain, BamA, as well as in the lipoprotein BamC. We have used cellular solid-state NMR spectroscopy to examine the entire BamABCDE complex in native outer membranes and obtained data on the BamCDE subcomplex in outer membranes, in addition to synthetic bilayers. To reduce spectral crowding, we utilized proton-detected experiments and employed amino-acid specific isotope-labelling in (13C, 13C) correlation experiments. Taken together, the results provide insight into the overall fold and assembly of the BAM complex in native membranes, in particular regarding the structural flexibility of BamC in the absence of the core unit BamA

KW - Solid-state NMR

KW - BAM

KW - MAS

KW - E. coli

KW - Membrane protein complex

U2 - 10.1016/j.jsb.2017.11.015

DO - 10.1016/j.jsb.2017.11.015

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JO - Journal of Structural Biology

JF - Journal of Structural Biology

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Studying assembly of the BAM complex in native membranes by cellular solid-state NMR spectroscopy

Abstract

Keywords

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