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The domain structure of the ion channel-forming protein colicin Ia

Nature Structural Biology volume 1, pages 597–604 (1994)Cite this article

Abstract

Colicin Ia undergoes a transition from a soluble to a transmembrane state, forming an ion channel to effect its bactericidal activity. The X-ray crystal structure of soluble colicin Ia at an effective resolution of 4 Å reveals that the molecule is highly α-helical and has an unusually elongated ‘Y’-shape. The stalk and two arms of the ‘Y’ form three discrete structural domains which most likely correspond to the three functional regions identified for the channel-forming colicins. The channel-forming region of colicin Ia can be located to the larger of the two arms, the insertion domain, by its structural similarity to the ten α-helix motif found for the ion channel-forming fragments of colicins A and E1. The domain arrangement found in this structure provides novel insights into the mechanism of membrane insertion of colicin Ia.

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Author information

Author notes

  1. Partho Ghosh

    Present address: Department of Biochemistry and Molecular Biology, Harvard University, 7 Divinity Avenue, Cambridge, MA, 02138

  2. Stephanie F. Mel

    Present address: Department of Microbiology and Molecular Genetics, Harvard Medical School, 200 Longwood Avenue, Boston, MA, 02115

Authors and Affiliations

  1. Departments of Biochemistry and Biophysics, University of California, San Francisco, California, 94143-0448, USA

    Robert M. Stroud

  2. Department of Experimental Pathology, University of California, San Francisco, California, 94143-0448, USA

    Stephanie F. Mel

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  1. Partho Ghosh
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  3. Robert M. Stroud
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Ghosh, P., Mel, S. & Stroud, R. The domain structure of the ion channel-forming protein colicin Ia. Nat Struct Mol Biol 1, 597–604 (1994). https://doi.org/10.1038/nsb0994-597

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