THE DOMAIN-STRUCTURE OF THE ION CHANNEL-FORMING PROTEIN COLICIN IA

Colicin la 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 la at an effective resolution of 4 Angstrom 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 la can be located to the larger of the two arms, the insertion domain, by its structural similarity to the ten a-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 la.