期刊
NATURE STRUCTURAL & MOLECULAR BIOLOGY
卷 20, 期 2, 页码 159-166出版社
NATURE PUBLISHING GROUP
DOI: 10.1038/nsmb.2473
关键词
-
资金
- NRSA postdoctoral fellowship from the US National Institutes of Health [F32GM087865]
- National Institutes of Health [RO1GM088352]
Understanding how ion channels open and close their pores is crucial for comprehending their physiological roles. We used intracellular quaternary ammonium blockers, electrophysiology and X-ray crystallography to locate the voltage-dependent gate in MthK potassium channels from Methanobacterium thermoautotrophicum. Blockers bind in an aqueous cavity between two putative gates: an intracellular gate and the selectivity filter. Thus, these blockers directly probe gate location an intracellular gate will prevent binding when closed, whereas a selectivity filter gate will always allow binding. Kinetic analysis of tetrabutylammonium block of single MthK channels combined with X-ray crystallographic analysis of the pore with tetrabutyl antimony unequivocally determined that the voltage-dependent gate, like the C-type inactivation gate in eukaryotic channels, is located at the selectivity filter. State-dependent binding kinetics suggest that MthK inactivation leads to conformational changes within the cavity and intracellular pore entrance.
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