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    Intrinsically disordered protein threads through the bacterial outer-membrane Porin OmpF

    Housden, N.G. and Hopper, J.T.S. and Lukoyanova, Natalya and Rodriguez-Larrea, D. and Wojdyla, J.A. and Klein, A. and Kaminska, R. and Bayley, H. and Saibil, Helen R. and Robinson, C.V. and Kleanthous, C. (2013) Intrinsically disordered protein threads through the bacterial outer-membrane Porin OmpF. Science 340 (6140), pp. 1570-1574. ISSN 0036-8075.

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    Abstract

    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.

    Metadata

    Item Type: Article
    School: Birkbeck Schools and Departments > School of Science > Biological Sciences
    Research Centre: Structural Molecular Biology, Institute of (ISMB)
    Depositing User: Administrator
    Date Deposited: 23 Apr 2015 07:08
    Last Modified: 06 Dec 2016 11:14
    URI: http://eprints.bbk.ac.uk/id/eprint/11959

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