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Porins are β-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.

Original publication

DOI

10.1126/science.1237864

Type

Journal article

Journal

Science

Publication Date

28/06/2013

Volume

340

Pages

1570 - 1574

Keywords

Cell Membrane, Colicins, Escherichia coli, Escherichia coli Proteins, Periplasmic Proteins, Porins, Protein Multimerization, Protein Structure, Tertiary, Protein Transport