Potassium permeation through the KcsA channel: a density functional study

Biochim Biophys Acta. 2002 Jun 13;1563(1-2):1-6. doi: 10.1016/s0005-2736(02)00349-8.

Abstract

We present a theoretical study on structural and electronic aspects of K+ permeation through the binding sites of the KcsA channel's selectivity filter. Density functional calculations are carried out on models taken from selected snapshots of a molecular dynamics simulation recently reported [FEBS Lett. 477 (2000) 37]. During the translocation process from one binding site to the other, the coordination number of the permeating K+ ion turns out to decrease and K+ ion polarizes significantly its ligands, backbone carbonyl groups and a water molecule. K+-induced polarization increases significantly at the transition state (TS) between the two binding sites. These findings suggest that polarization effects play a significant role in the microscopic mechanisms regulating potassium permeation.

Publication types

  • Research Support, U.S. Gov't, P.H.S.

MeSH terms

  • Bacterial Proteins*
  • Binding Sites
  • Cations, Monovalent
  • Ion Transport
  • Ligands
  • Models, Molecular
  • Potassium / chemistry*
  • Potassium Channels / chemistry*
  • Quantum Theory
  • Streptomyces

Substances

  • Bacterial Proteins
  • Cations, Monovalent
  • Ligands
  • Potassium Channels
  • prokaryotic potassium channel
  • Potassium