Refolding of Escherichia coli outer membrane protein F in detergent creates LPS-free trimers and asymmetric dimers.

ABSTRACT: The Escherichia coli OmpF (outer-membrane protein F; matrix porin) is a homotrimeric beta-barrel and a member of the bacterial porin superfamily. It is the best characterized porin protein, but has resisted attempts to refold it efficiently in vitro. In the present paper, we report the discovery of detergent-based folding conditions, including dodecylglucoside, which can create pure samples of trimeric OmpF. Whereas outer membrane LPS (lipopolysaccharide) is clearly required for in vivo folding, the artificially refolded and LPS-free trimer has properties identical with those of the outer-membrane-derived form. Thus LPS is not required either for in vitro folding or for structural integrity. Dimeric forms of OmpF have been observed in vivo and are proposed to be folding intermediates. In v

SUBMITTER: Visudtiphole V 

PROVIDER: S-EPMC1316273 | biostudies-literature | 2005 Dec

REPOSITORIES: biostudies-literature