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Crystal structure of colicin Ia

Nature volume 385, pages 461–464 (1997)Cite this article

Abstract

The ion-channel forming colicins A, B, El, Ia, Ib and N all kill bacterial cells selectively by co-opting bacterial active-transport pathways and forming voltage-gated ion conducting channels across the plasma membrane of the target bacterium1,2. The crystal structure of colicin Ia reveals a molecule 210 Å long with three distinct functional domains arranged along a backbone of two extraordinarily long α-helices. A central domain at the bend of the hairpin-like structure mediates specific recognition and binding to an outer-membrane receptor3. A second domain mediates translocation across the outer membrane via the TonB transport pathway4; the TonB-box5 recognition element of colicin Ia is on one side of three 80 Å-long helices arranged as a helical sheet. A third domain is made up of 10 α-helices which form a voltage-activated and voltage-gated ion conducting channel across the plasma membrane of the target cell. The two 160 Å-long α-helices that link the receptor-binding domain to the other domains enable the colicin Ia molecule to span the periplasmic space and contact both the outer and plasma membranes simultaneously during function6,7.

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Author notes

  1. Michael Wiener

    Present address: Department of Molecular Physiology and Biological Physics, University of Virginia Health Sciences Center, PO Box 10011, Charlottesville, Virginia, 22906-0011, USA

  2. Partho Ghosh

    Present address: Department of Molecular and Cellular Biology, Harvard University, 7 Divinity Avenue, Cambridge, Massachusetts, 02138, USA

Authors and Affiliations

  1. S-964 Department of Biochemistry and Biophysics, University of California, San Francisco, California, 94143-0448, USA

    Michael Wiener, Douglas Freymann, Partho Ghosh & Robert M. Stroud

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  1. Michael Wiener
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  2. Douglas Freymann
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  3. Partho Ghosh
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  4. Robert M. Stroud
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Wiener, M., Freymann, D., Ghosh, P. et al. Crystal structure of colicin Ia. Nature 385, 461–464 (1997). https://doi.org/10.1038/385461a0

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