Molecular Movement of the Voltage Sensor in a K Channel

Amir Broomand, Roope Männikkö, Hans P Larsson, Fredrik Elinder

Research output: Contribution to journalArticle

58 Citations (Scopus)

Abstract

The X-ray crystallographic structure of KvAP, a voltage-gated bacterial K channel, was recently published. However, the position and the molecular movement of the voltage sensor, S4, are still controversial. For example, in the crystallographic structure, S4 is located far away (>30 Å) from the pore domain, whereas electrostatic experiments have suggested that S4 is located close (<8 Å) to the pore domain in open channels. To test the proposed location and motion of S4 relative to the pore domain, we induced disulphide bonds between pairs of introduced cysteines: one in S4 and one in the pore domain. Several residues in S4 formed a state-dependent disulphide bond with a residue in the pore domain. Our data suggest that S4 is located close to the pore domain in a neighboring subunit. Our data also place constraints on possible models for S4 movement and are not compatible with a recently proposed KvAP model.

Original languageEnglish
Pages (from-to)741-748
Number of pages8
JournalJournal of General Physiology
Volume122
Issue number6
DOIs
StatePublished - Dec 1 2003
Externally publishedYes

Fingerprint

Disulfides
Pair Bond
Voltage-Gated Potassium Channels
Static Electricity
Cysteine
X-Rays

Keywords

  • Disulfide
  • Helical screw
  • S4 movement
  • Shaker K channel
  • Voltage gated

ASJC Scopus subject areas

  • Physiology

Cite this

Molecular Movement of the Voltage Sensor in a K Channel. / Broomand, Amir; Männikkö, Roope; Larsson, Hans P; Elinder, Fredrik.

In: Journal of General Physiology, Vol. 122, No. 6, 01.12.2003, p. 741-748.

Research output: Contribution to journalArticle

Broomand, Amir ; Männikkö, Roope ; Larsson, Hans P ; Elinder, Fredrik. / Molecular Movement of the Voltage Sensor in a K Channel. In: Journal of General Physiology. 2003 ; Vol. 122, No. 6. pp. 741-748.
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