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Nat Struct Biol. 1994 Sep;1(9):597-604.

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

Author information

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

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 A reveals that the molecule is highly alpha-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 alpha-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.

PMID:
7543362
DOI:
10.1038/nsb0994-597
[Indexed for MEDLINE]

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