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PLoS Biol. 2007 May;5(5):e121.

Structural and thermodynamic properties of selective ion binding in a K+ channel.

Author information

1
Laboratory of Molecular Neurobiology and Biophysics, The Rockefeller University, New York, New York, United States of America.

Abstract

Thermodynamic measurements of ion binding to the Streptomyces lividans K(+) channel were carried out using isothermal titration calorimetry, whereas atomic structures of ion-bound and ion-free conformations of the channel were characterized by x-ray crystallography. Here we use these assays to show that the ion radius dependence of selectivity stems from the channel's recognition of ion size (i.e., volume) rather than charge density. Ion size recognition is a function of the channel's ability to adopt a very specific conductive structure with larger ions (K(+), Rb(+), Cs(+), and Ba(2+)) bound and not with smaller ions (Na(+), Mg(2+), and Ca(2+)). The formation of the conductive structure involves selectivity filter atoms that are in direct contact with bound ions as well as protein atoms surrounding the selectivity filter up to a distance of 15 A from the ions. We conclude that ion selectivity in a K(+) channel is a property of size-matched ion binding sites created by the protein structure.

PMID:
17472437
PMCID:
PMC1858713
DOI:
10.1371/journal.pbio.0050121
[Indexed for MEDLINE]
Free PMC Article

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