FEBS Letters | |
Exploring the open pore of the potassium channel from Streptomyces lividans | |
Meuser, D.2  Wagner, R.1  Splitt, H.2  Schrempf, H.2  | |
[1] Biophysik, FB Biologie/Chemie, Universität Osnabrück, 49069 Osnabrück, Germany;Angewandte Genetik der Mikroorganismen, Universität Osnabrück, 49069 Osnabrück, Germany | |
关键词: Block; Ion permeation; KcsA; Pore; Potassium channel; Streptomyces lividans; DDM; dodecylmaltoside; QA; quaternary ammonium ion; TBA; tetrabutylammonium; TEA; tetraethylammonium; THepA; tetraheptylammonium; THexA; tetrahexylammonium; TM; transmembrane; TMA; tetramethylammonium; TPrA; tetrapropylammonium; TPenA; tetrapentylammonium; | |
DOI : 10.1016/S0014-5793(99)01579-3 | |
学科分类:生物化学/生物物理 | |
来源: John Wiley & Sons Ltd. | |
【 摘 要 】
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 (n H2O≳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 ∼5.8 Å. 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.
【 授权许可】
Unknown
【 预 览 】
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