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

Housden, NG; Hopper, JT; Lukoyanova, N; Rodriguez-Larrea, D; Wojdyla, JA; Klein, A; Kaminska, R; Bayley, H; Saibil, HR; Robinson, CV; Kleanthous, C

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 membr...

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APA Style

Housden, N. G., Hopper, J. T., Lukoyanova, N., Rodriguez-Larrea, D., Wojdyla, J. A., Klein, A., Kaminska, R., Bayley, H., Saibil, H. R., Robinson, C. V., & Kleanthous, C. (2013). Intrinsically disordered protein threads through the bacterial outer-membrane porin OmpF. Science (New York, N.Y.), 340(6140), 1570–1574.

MLA Style

Housden, N. G., et al. “Intrinsically Disordered Protein Threads through the Bacterial Outer-Membrane Porin OmpF.” Science (New York, N.Y.), vol. 340, no. 6140, Science (New York, N.Y.), 2013, pp. 1570–74.

Chicago Style

Housden, NG, JT Hopper, N Lukoyanova, D Rodriguez-Larrea, JA Wojdyla, A Klein, R Kaminska, et al. 2013. “Intrinsically Disordered Protein Threads through the Bacterial Outer-Membrane Porin OmpF.” Science (New York, N.Y.) 340 (6140): 1570–74.
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