Exploring the open pore of the potassium channel fromStreptomyces lividans
| Autor: | Heiner Splitt, Hildgund Schrempf, Richard Wagner, Dirk Meuser |
|---|---|
| Rok vydání: | 1999 |
| Předmět: |
Ion permeation
Potassium Channels Protein Conformation Inorganic chemistry Block Biophysics KcsA potassium channel Gating Crystal structure Biochemistry Permeability Membrane Potentials Ion Bacterial Proteins Structural Biology Electric field Escherichia coli Genetics KcsA Potassium channel Molecular Biology Pore Chemistry Cell Biology Thermal conduction Streptomyces Electrophysiology Quaternary Ammonium Compounds Crystallography Barium Mutagenesis Potassium Streptomyces lividans Selectivity |
| Zdroj: | FEBS Letters. 462:447-452 |
| ISSN: | 0014-5793 |
| DOI: | 10.1016/s0014-5793(99)01579-3 |
| Popis: | The tetrameric potassium channel from Streptomyces lividans (KcsA) embedded in planar bilayers exhibits the following electrophysiological characteristics: (i) K+ ions can cross the pore in a highly hydrated state (nH2Oor = 6), (ii) the selectivity for K+ exceeds that for Na+ ions by 11 times, and both Ca2+ and Mg2+ are permeant, (iii) the internal side is blocked by Ba2+ ions in a voltage-dependent manner, (iv) intrinsic rectification is due to gating, depending on the direction of the electric field, (v) the internal side is pH-sensitive, and (vi) the open pore has a diameter of approximately 5.8 A. In conclusion, our results show that ion conduction and selectivity of KcsA cannot easily be reconciled with the properties deduced from the rigid crystal structure [Doyle et al., Science 280 (1998) 69-77], which must be concluded to have the pore trapped in its closed state. |
| Databáze: | OpenAIRE |
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