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Chembiochem. 2014 Sep 22;15(14):2113-24. doi: 10.1002/cbic.201402162. Epub 2014 Aug 19.

Low-resolution structures of OmpA⋅DDM protein-detergent complexes.

Author information

1
Interdisciplinary Nanoscience Center (iNANO), Aarhus University, Gustav Wieds Vej 14, 8000 Aarhus C (Denmark); Department of Chemistry, Aarhus University, Langelandsgade 140, 8000 Aarhus C (Denmark).

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.

KEYWORDS:

membrane proteins; micelles; outer-membrane protein A; protein/detergent stoichiometry; small-angle X-ray scattering

PMID:
25138961
DOI:
10.1002/cbic.201402162
[Indexed for MEDLINE]

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