Simplified bacterial "pore" channel provides insight into the assembly, stability, and structure of sodium channels.

ABSTRACT: Eukaryotic sodium channels are important membrane proteins involved in ion permeation, homeostasis, and electrical signaling. They are long, multidomain proteins that do not express well in heterologous systems, and hence, structure/function and biochemical studies on purified sodium channel proteins have been limited. Bacteria produce smaller, homologous tetrameric single domain channels specific for the conductance of sodium ions. They consist of N-terminal voltage sensor and C-terminal pore subdomains. We designed a functional pore-only channel consisting of the final two transmembrane helices, the intervening P-region, and the C-terminal extramembranous region of the sodium channel from the marine bacterium Silicibacter pomeroyi. This sodium "pore" channel forms a tetrameric, folded st

SUBMITTER: McCusker EC 

PROVIDER: S-EPMC3091244 | biostudies-literature | 2011 May

REPOSITORIES: biostudies-literature