Abstract
The determination of the crystal structure of the bacterial protein proaerolysin provided the first view of a pore-forming toxin constructed mainly from beta-sheet. The structure that was obtained and subsequent crystallographic and biochemical studies have together allowed us to explain how the toxin is transformed from a water-soluble dimer to a heptameric transmembrane pore. Recent discoveries of structural similarities between aerolysin and other toxins suggest that the structure/function studies we have made may prove useful in understanding the actions of a number of pore- forming proteins.
Original language | English |
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Pages (from-to) | 92-100 |
Number of pages | 9 |
Journal | Journal of Structural Biology |
Volume | 121 |
Issue number | 2 |
DOIs | |
Publication status | Published - 1 Jan 1998 |
Externally published | Yes |
Keywords
- Aerolysin
- Membrane channels
- Membrane insertion
- Protein toxins
- X-ray crystallography