Ontology highlight
ABSTRACT:
SUBMITTER: Rotem D
PROVIDER: S-EPMC2806417 | biostudies-literature | 2010 Jan
REPOSITORIES: biostudies-literature
Rotem Dvir D Mason Amy A Bayley Hagan H
The Journal of general physiology 20100101 1
The tetrameric prokaryotic potassium channel KcsA is activated by protons acting on the intracellular aspect of the protein and inactivated through conformational changes in the selectivity filter. Inactivation is modulated by a network of interactions within each protomer between the pore helix and residues at the external entrance of the channel. Inactivation is suppressed by the E71A mutation, which perturbs the stability of this network. Here, cell-free protein synthesis followed by protein ...[more]