Potassium and sodium binding to the outer mouth of the K+ channel.
Molecular dynamics simulations of the K+ channel from Streptomyces lividans (KcsA channel) were performed in a membrane-mimetic environment with Na+ and K+ in different initial locations. The structure of the channel remained stable and well preserved for simulations lasting up to 1.5 ns. Salt bridges between Asp80 and Arg89 of neighboring subunits, not detected in the X-ray structure, enhanced the stability of the tetrameric structure. Na+ or K+ ions located in the channel vestibule lost part of their hydration shell and diffused into the channel inner pore in less than a few hundred picoseconds. This powerful catalytic action was caused by strong electrostatic interactions with Asp80 and Glu71. The hydration state of the metal ions turned out to depend significantly on the conformational flexibility of the channel. Furthermore, Na+ entered the channel inner pore bound to more water molecules than K+. The different hydration state of the two ions may be a determinant factor in the ion selectivity of the channel.
Scuola Internazionale Superiore di Studi Avanzati, Istituto Nazionale di Fisica della Materia, Trieste, Italy.
L
L
Guidoni
V
V
Torre
P
P
Carloni
D001665:Binding Sites; D003198:Computer Simulation; D018360:Crystallography, X-Ray; D008958:Models, Molecular; D011188:Potassium / Q000737:chemistry / Q000378:metabolism*; D015221:Potassium Channels / Q000737:chemistry / Q000378:metabolism*; D011487:Protein Conformation; D012964:Sodium / Q000737:chemistry / Q000378:metabolism*; D055672:Static Electricity; D013302:Streptomyces / Q000737:chemistry; D013329:Structure-Activity Relationship; D013816:Thermodynamics
D015221:Potassium Channels; D012964:Sodium; D011188:Potassium