Probing the Structural Dynamics of the Activation Gate of KcsA Using Homo-FRET Measurements.

ABSTRACT: The allosteric coupling between activation and inactivation processes is a common feature observed in K⁺ channels. Particularly, in the prokaryotic KcsA channel the K⁺ conduction process is controlled by the inner gate, which is activated by acidic pH, and by the selectivity filter (SF) or outer gate, which can adopt non-conductive or conductive states. In a previous study, a single tryptophan mutant channel (W67 KcsA) enabled us to investigate the SF dynamics using time-resolved homo-Förster Resonance Energy Transfer (homo-FRET) measurements. Here, the conformational changes of both gates were simultaneously monitored after labelling the G116C position with tetramethylrhodamine (TMR) within a W67 KcsA background. At a high degree of protein labeling, fluorescence ani

SUBMITTER: Diaz-Garcia C 

PROVIDER: S-EPMC8584343 | biostudies-literature | 2021 Nov

REPOSITORIES: biostudies-literature