Hertel, Brigitte ; Tayefeh, Sascha ; Kloss, Thomas ; Hewing, Jennifer ; Gebhardt, Manuela ; Baumeister, Dirk ; Moroni, Anna ; Thiel, Gerhard ; Kast, Stefan M. (2010)
Salt bridges in the miniature viral channel Kcv are important for function.
In: European biophysics journal : EBJ, 39 (7)
Artikel, Bibliographie
Kurzbeschreibung (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.
| Typ des Eintrags: | Artikel |
|---|---|
| Erschienen: | 2010 |
| Autor(en): | Hertel, Brigitte ; Tayefeh, Sascha ; Kloss, Thomas ; Hewing, Jennifer ; Gebhardt, Manuela ; Baumeister, Dirk ; Moroni, Anna ; Thiel, Gerhard ; Kast, Stefan M. |
| Art des Eintrags: | Bibliographie |
| Titel: | Salt bridges in the miniature viral channel Kcv are important for function. |
| Sprache: | Englisch |
| Publikationsjahr: | 2010 |
| Titel der Zeitschrift, Zeitung oder Schriftenreihe: | European biophysics journal : EBJ |
| Jahrgang/Volume einer Zeitschrift: | 39 |
| (Heft-)Nummer: | 7 |
| Kurzbeschreibung (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. |
| Fachbereich(e)/-gebiet(e): | 10 Fachbereich Biologie > Plant Membrane Biophyscis (am 20.12.23 umbenannt in Biologie der Algen und Protozoen) ?? fb10_botanik ?? 10 Fachbereich Biologie |
| Hinterlegungsdatum: | 21 Jun 2011 12:04 |
| Letzte Änderung: | 05 Mär 2013 09:49 |
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