| THE DOMAIN-STRUCTURE OF THE ION CHANNEL-FORMING PROTEIN COLICIN IA |
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| Author(s): GHOSH P, MEL SF, STROUD RM |
| Source: NATURE STRUCTURAL BIOLOGY Volume: 1 Issue: 9 Pages: 597-604 Published: SEP 1994 |
| Times Cited: 25 References: 44 |
| Abstract: 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. |
| Document Type: Article |
| Language: English |
Addresses:
1. UNIV CALIF SAN FRANCISCO, DEPT BIOCHEM & BIOPHYS, SAN FRANCISCO, CA 94143 USA
2. UNIV CALIF SAN FRANCISCO, DEPT EXPTL PATHOL, SAN FRANCISCO, CA 94143 USA |
| Publisher: NATURE PUBLISHING CO, 345 PARK AVE SOUTH, NEW YORK, NY 10010-1707 |
| Subject Category: Biochemistry & Molecular Biology; Biophysics; Cell Biology |
| IDS Number: PJ449 |
| ISSN: 1072-8368 |