Article
The molecular basis for the pH-activation mechanism in the channel-forming bacterial colicin E1.
The Journal of biological chemistry - 4 Jul 2003
Musse Abdiwahab A, Merrill A Rod
Abstract excerpt
The in vitro activity of the channel-forming bacteriocins such as colicin E1 in model membranes requires the specific activation of the protein by an acidic environment in the presence of a membrane potential. Acid activation of the C-terminal domain results in the formation of an insertion-competent intermediate with an enhanced ability to penetrate and perforate cell membranes. We report novel findings of this...
Topics
- Amino Acid Sequence
- Colicins
- Escherichia coli
- Hydrogen-Ion Concentration
- Models, Molecular
- Molecular Sequence Data
- Mutation
- Protein Conformation
- Sequence Alignment