The structure of the potassium channel: molecular basis of K+ conduction and selectivity
- PMID: 9525859
- DOI: 10.1126/science.280.5360.69
The structure of the potassium channel: molecular basis of K+ conduction and selectivity
Abstract
The potassium channel from Streptomyces lividans is an integral membrane protein with sequence similarity to all known K+ channels, particularly in the pore region. X-ray analysis with data to 3.2 angstroms reveals that four identical subunits create an inverted teepee, or cone, cradling the selectivity filter of the pore in its outer end. The narrow selectivity filter is only 12 angstroms long, whereas the remainder of the pore is wider and lined with hydrophobic amino acids. A large water-filled cavity and helix dipoles are positioned so as to overcome electrostatic destabilization of an ion in the pore at the center of the bilayer. Main chain carbonyl oxygen atoms from the K+ channel signature sequence line the selectivity filter, which is held open by structural constraints to coordinate K+ ions but not smaller Na+ ions. The selectivity filter contains two K+ ions about 7.5 angstroms apart. This configuration promotes ion conduction by exploiting electrostatic repulsive forces to overcome attractive forces between K+ ions and the selectivity filter. The architecture of the pore establishes the physical principles underlying selective K+ conduction.
Comment in
- Science. 1998 Aug 14;281(5379):883
-
The vision of the pore.Science. 1998 Apr 3;280(5360):56-7. doi: 10.1126/science.280.5360.56. Science. 1998. PMID: 9556453 No abstract available.
-
A vision of the pore.Science. 1998 Aug 21;281(5380):1146. doi: 10.1126/science.281.5380.1143h. Science. 1998. PMID: 9735029 No abstract available.
Similar articles
-
The cavity and pore helices in the KcsA K+ channel: electrostatic stabilization of monovalent cations.Science. 1999 Jul 2;285(5424):100-2. doi: 10.1126/science.285.5424.100. Science. 1999. PMID: 10390357
-
The vision of the pore.Science. 1998 Apr 3;280(5360):56-7. doi: 10.1126/science.280.5360.56. Science. 1998. PMID: 9556453 No abstract available.
-
Molecular dynamics of the KcsA K(+) channel in a bilayer membrane.Biophys J. 2000 Jun;78(6):2900-17. doi: 10.1016/S0006-3495(00)76831-7. Biophys J. 2000. PMID: 10827971 Free PMC article.
-
The potassium channel KcsA and its interaction with the lipid bilayer.Cell Mol Life Sci. 2003 Aug;60(8):1581-90. doi: 10.1007/s00018-003-3172-y. Cell Mol Life Sci. 2003. PMID: 14513833 Free PMC article. Review.
-
Ion selectivity in potassium channels.Biophys Chem. 2006 Dec 1;124(3):279-91. doi: 10.1016/j.bpc.2006.05.033. Epub 2006 Jun 18. Biophys Chem. 2006. PMID: 16843584 Review.
Cited by
-
Poring over two-pore channel pore mutants.Messenger (Los Angel). 2015 Jun 1;4(1):46-52. doi: 10.1166/msr.2015.1044. Messenger (Los Angel). 2015. PMID: 27226934 Free PMC article.
-
CAVER 3.0: a tool for the analysis of transport pathways in dynamic protein structures.PLoS Comput Biol. 2012;8(10):e1002708. doi: 10.1371/journal.pcbi.1002708. Epub 2012 Oct 18. PLoS Comput Biol. 2012. PMID: 23093919 Free PMC article.
-
ICA-105574 interacts with a common binding site to elicit opposite effects on inactivation gating of EAG and ERG potassium channels.Mol Pharmacol. 2013 Apr;83(4):805-13. doi: 10.1124/mol.112.084384. Epub 2013 Jan 14. Mol Pharmacol. 2013. PMID: 23319419 Free PMC article.
-
Voltage-Gated Potassium Channels: A Structural Examination of Selectivity and Gating.Cold Spring Harb Perspect Biol. 2016 May 2;8(5):a029231. doi: 10.1101/cshperspect.a029231. Cold Spring Harb Perspect Biol. 2016. PMID: 27141052 Free PMC article. Review.
-
Molecular bases of NMDA receptor subtype-dependent properties.J Physiol. 2015 Jan 1;593(1):83-95. doi: 10.1113/jphysiol.2014.273763. Epub 2014 Sep 9. J Physiol. 2015. PMID: 25556790 Free PMC article. Review.
Publication types
MeSH terms
Substances
LinkOut - more resources
Full Text Sources
Other Literature Sources
Medical
Molecular Biology Databases