Intrinsically disordered protein threads through the bacterial outer-membrane porin OmpF. (2013)

Abstract

Porins are ß-barrel outer-membrane proteins through which small solutes and metabolites diffuse that are also exploited during cell death. We have studied how the bacteriocin colicin E9 (ColE9) assembles a cytotoxic translocon at the surface of Escherichia coli that incorporates the trimeric porin OmpF. Formation of the translocon involved ColE9's unstructured N-terminal domain threading in opposite directions through two OmpF subunits, capturing its target TolB on the other side of the membrane in a fixed orientation that triggers colicin import. Thus, an intrinsically disordered protein can tunnel through the narrow pores of an oligomeric porin to deliver an epitope signal to the cell to initiate cell death.

Bibliographic Information

Digital Object Identifier: http://dx.doi.org/10.1126/science.1237864

PubMed Identifier: 23812713

Publication URI: http://europepmc.org/abstract/MED/23812713

Type: Journal Article/Review

Volume: 340

Parent Publication: Science (New York, N.Y.)

Issue: 6140

ISSN: 0036-8075