Article
Rearrangements in the KcsA cytoplasmic domain underlie its gating.
The Journal of biological chemistry - 5 Feb 2010
Hirano Minako, Takeuchi Yuko, Aoki Takaaki, Yanagida Toshio, Ide Toru
Abstract excerpt
A change of cytosolic pH 7 to 4 opens the bacterial potassium channel KcsA. However, the overall gating mechanism leading to channel opening, especially the contribution of the cytoplasmic domain, remains unsolved. Here we report that deletion of the cytoplasmic domain resulted in changes in channel conductance and gating behavior at pH 4 without channel opening at pH 7. To probe for rearrangements in the...
Topics
- Bacterial Proteins
- Binding Sites
- Fluorescence Resonance Energy Transfer
- Hydrogen-Ion Concentration
- Ion Channel Gating
- Lipid Bilayers
- Liposomes
- Membrane Potentials
- Mutagenesis, Site-Directed
- Mutation
- Potassium Channels
- Protein Conformation
- Protein Structure, Tertiary
- Rhodamines