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Issue 24, 2005
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Role of water molecules in the KcsA protein channel by molecular dynamics calculations

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Abstract

Molecular dynamics simulations supported by electrostatic calculations have been conducted on the KcsA channel to determine the role of water molecules in the pore. Starting from the X-ray structure of the KcsA channel in its closed state at 2.0 Å resolution, the opening of the pore towards a conformation built on the basis of EPR results is studied. We show that water molecules act as a structural element for the K+ ions inside the filter and the hydrophobic cavity of the channel. In the filter, water tends to enhance the depth of the wells occupied by the K+ ions, while in the cavity there is a strong correlation between the water molecules and the cavity ion. As a consequence, the protein remains very stable in the presence of three K+ ions in the selectivity filter and one in the cavity. The analysis of the dynamics of water molecules in the cavity reveals preferred orientations of the dipoles along the pore axis, and a correlated behavior between this dipole orientation and the displacement of the K+ ion during the gating process.

Graphical abstract: Role of water molecules in the KcsA protein channel by molecular dynamics calculations

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Article information


Submitted
10 Jun 2005
Accepted
15 Sep 2005
First published
06 Oct 2005

Phys. Chem. Chem. Phys., 2005,7, 4138-4145
Article type
Paper

Role of water molecules in the KcsA protein channel by molecular dynamics calculations

M. Compoint, C. Boiteux, P. Huetz, C. Ramseyer and C. Girardet, Phys. Chem. Chem. Phys., 2005, 7, 4138
DOI: 10.1039/B508281A

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