Low-Resolution Structures of OmpA⋅DDM Protein-Detergent Complexes

Jørn Kaspersen; Christian Moestrup Jessen; Brian Stougaard Vad; Esben Skipper Sørensen; Kell Kleiner Andersen; Marianne Glasius; Cristiano Luis Pinto Oliveira; Daniel Otzen; Jan Skov Pedersen

doi:10.1002/cbic.201402162

Low-Resolution Structures of OmpA⋅DDM Protein-Detergent Complexes

Jørn Kaspersen, Christian Moestrup Jessen, Brian Stougaard Vad, Esben Skipper Sørensen, Kell Kleiner Andersen, Marianne Glasius, Cristiano Luis Pinto Oliveira, Daniel Otzen, Jan Skov Pedersen

Research output: Contribution to journal/Conference contribution in journal/Contribution to newspaper › Journal article › Research › peer-review

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Abstract

We have used SAXS to determine the low-resolution structure of the outer-membrane protein OmpA from E. coli solubilized by the surfactant dodecyl maltoside (DDM). We have studied three variants of the transmembrane domain of OmpA-namely monomers, self-associated dimers, and covalently linked dimers-as well as the monomeric species of the full-length protein with the periplasmic domain. We can successfully model the structures of the monomeric and covalently linked dimer as one and two natively folded proteins in a DDM micelle, respectively, whereas the noncovalently linked dimer presents a more complicated structure, possibly due to higher-order species. We have determined the structure of the full-length protein to be that of a globular periplasmic domain attached through a flexible linker to the transmembrane domain. This approach provides valuable information about how membrane proteins are embedded in amphiphilic environments.

Original language	English
Journal	ChemBioChem
Volume	15
Issue	14
Pages (from-to)	2113-2124
Number of pages	12
ISSN	1439-4227
DOIs	https://doi.org/10.1002/cbic.201402162
Publication status	Published - 19 Aug 2014

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title = "Low-Resolution Structures of OmpA⋅DDM Protein-Detergent Complexes",

abstract = "We have used SAXS to determine the low-resolution structure of the outer-membrane protein OmpA from E. coli solubilized by the surfactant dodecyl maltoside (DDM). We have studied three variants of the transmembrane domain of OmpA-namely monomers, self-associated dimers, and covalently linked dimers-as well as the monomeric species of the full-length protein with the periplasmic domain. We can successfully model the structures of the monomeric and covalently linked dimer as one and two natively folded proteins in a DDM micelle, respectively, whereas the noncovalently linked dimer presents a more complicated structure, possibly due to higher-order species. We have determined the structure of the full-length protein to be that of a globular periplasmic domain attached through a flexible linker to the transmembrane domain. This approach provides valuable information about how membrane proteins are embedded in amphiphilic environments.",

author = "J{\o}rn Kaspersen and {Moestrup Jessen}, Christian and {Stougaard Vad}, Brian and {Skipper S{\o}rensen}, Esben and {Kleiner Andersen}, Kell and Marianne Glasius and {Pinto Oliveira}, {Cristiano Luis} and Daniel Otzen and Pedersen, {Jan Skov}",

note = "{\textcopyright} 2014 WILEY-VCH Verlag GmbH & Co. KGaA, Weinheim.",

year = "2014",

month = aug,

day = "19",

doi = "10.1002/cbic.201402162",

language = "English",

volume = "15",

pages = "2113--2124",

journal = "ChemBioChem",

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publisher = "John Wiley & Sons Inc.",

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T1 - Low-Resolution Structures of OmpA⋅DDM Protein-Detergent Complexes

AU - Kaspersen, Jørn

AU - Moestrup Jessen, Christian

AU - Stougaard Vad, Brian

AU - Skipper Sørensen, Esben

AU - Kleiner Andersen, Kell

AU - Glasius, Marianne

AU - Pinto Oliveira, Cristiano Luis

AU - Otzen, Daniel

AU - Pedersen, Jan Skov

PY - 2014/8/19

Y1 - 2014/8/19

N2 - We have used SAXS to determine the low-resolution structure of the outer-membrane protein OmpA from E. coli solubilized by the surfactant dodecyl maltoside (DDM). We have studied three variants of the transmembrane domain of OmpA-namely monomers, self-associated dimers, and covalently linked dimers-as well as the monomeric species of the full-length protein with the periplasmic domain. We can successfully model the structures of the monomeric and covalently linked dimer as one and two natively folded proteins in a DDM micelle, respectively, whereas the noncovalently linked dimer presents a more complicated structure, possibly due to higher-order species. We have determined the structure of the full-length protein to be that of a globular periplasmic domain attached through a flexible linker to the transmembrane domain. This approach provides valuable information about how membrane proteins are embedded in amphiphilic environments.

AB - We have used SAXS to determine the low-resolution structure of the outer-membrane protein OmpA from E. coli solubilized by the surfactant dodecyl maltoside (DDM). We have studied three variants of the transmembrane domain of OmpA-namely monomers, self-associated dimers, and covalently linked dimers-as well as the monomeric species of the full-length protein with the periplasmic domain. We can successfully model the structures of the monomeric and covalently linked dimer as one and two natively folded proteins in a DDM micelle, respectively, whereas the noncovalently linked dimer presents a more complicated structure, possibly due to higher-order species. We have determined the structure of the full-length protein to be that of a globular periplasmic domain attached through a flexible linker to the transmembrane domain. This approach provides valuable information about how membrane proteins are embedded in amphiphilic environments.

U2 - 10.1002/cbic.201402162

DO - 10.1002/cbic.201402162

M3 - Journal article

C2 - 25138961

SN - 1439-4227

VL - 15

SP - 2113

EP - 2124

JO - ChemBioChem

JF - ChemBioChem

IS - 14

ER -

Low-Resolution Structures of OmpA⋅DDM Protein-Detergent Complexes

Abstract

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