Conformational plasticity in the KcsA potassium channel pore helix revealed by homo-FRET studies.

ABSTRACT: Potassium channels selectivity filter (SF) conformation is modulated by several factors, including ion-protein and protein-protein interactions. Here, we investigate the SF dynamics of a single Trp mutant of the potassium channel KcsA (W67) using polarized time-resolved fluorescence measurements. For the first time, an analytical framework is reported to analyze the homo-Förster resonance energy transfer (homo-FRET) within a symmetric tetrameric protein with a square geometry. We found that in the closed state (pH 7), the W67-W67 intersubunit distances become shorter as the average ion occupancy of the SF increases according to cation type and concentration. The hypothesis that the inactivated SF at pH 4 is structurally similar to its collapsed state, detected at low K⁺, pH 7, w

SUBMITTER: Renart ML 

PROVIDER: S-EPMC6470172 | biostudies-literature | 2019 Apr

REPOSITORIES: biostudies-literature