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Salt bridges in the miniature viral channel Kcv are important for function.

Hertel, Brigitte and Tayefeh, Sascha and Kloss, Thomas and Hewing, Jennifer and Gebhardt, Manuela and Baumeister, Dirk and Moroni, Anna and Thiel, Gerhard and Kast, Stefan M. (2010):
Salt bridges in the miniature viral channel Kcv are important for function.
In: European biophysics journal : EBJ, pp. 1057-68, 39, (7), ISSN 1432-1017,
[Article]

Abstract

The viral potassium channel Kcv comprises only 94 amino acids, which represent the pore module of more complex K(+) channels. As for Kir-type channels, Kcv also has a short N-terminal helix exposed to the cytoplasm, upstream of the first transmembrane domain. Here we show that this helix is relevant for Kcv function. The presence of charged amino acids, which form dynamic inter- and intra-subunit salt bridges is crucial. Electrophysiological measurements, yeast rescue experiments and molecular dynamics simulations show that mutants in which the critical salt bridge formation is impaired have no or reduced channel activity. We conclude that these salt bridges destabilise the complexation of K(+) ions by negative charges on the inner transmembrane domain at the entrance into the cavity. This feature facilitates a continuous and coordinated transfer of ions between the cavity and the cytoplasm for channels without the canonical bundle crossing.

Item Type: Article
Erschienen: 2010
Creators: Hertel, Brigitte and Tayefeh, Sascha and Kloss, Thomas and Hewing, Jennifer and Gebhardt, Manuela and Baumeister, Dirk and Moroni, Anna and Thiel, Gerhard and Kast, Stefan M.
Title: Salt bridges in the miniature viral channel Kcv are important for function.
Language: English
Abstract:

The viral potassium channel Kcv comprises only 94 amino acids, which represent the pore module of more complex K(+) channels. As for Kir-type channels, Kcv also has a short N-terminal helix exposed to the cytoplasm, upstream of the first transmembrane domain. Here we show that this helix is relevant for Kcv function. The presence of charged amino acids, which form dynamic inter- and intra-subunit salt bridges is crucial. Electrophysiological measurements, yeast rescue experiments and molecular dynamics simulations show that mutants in which the critical salt bridge formation is impaired have no or reduced channel activity. We conclude that these salt bridges destabilise the complexation of K(+) ions by negative charges on the inner transmembrane domain at the entrance into the cavity. This feature facilitates a continuous and coordinated transfer of ions between the cavity and the cytoplasm for channels without the canonical bundle crossing.

Journal or Publication Title: European biophysics journal : EBJ
Volume: 39
Number: 7
Divisions: 10 Department of Biology > Plant Membrane Biophysics
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10 Department of Biology
Date Deposited: 21 Jun 2011 12:04
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