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

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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.

OriginalsprogEngelsk
TidsskriftChemBioChem
Vol/bind15
Nummer14
Sider (fra-til)2113-2124
Antal sider12
ISSN1439-4227
DOI
StatusUdgivet - 19 aug. 2014

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