Crystal structure of the potassium channel KirBac1.1 in the closed state

Science. 2003 Jun 20;300(5627):1922-6. doi: 10.1126/science.1085028. Epub 2003 May 8.

Abstract

The KirBac1.1 channel belongs to the inward-rectifier family of potassium channels. Here we report the structure of the entire prokaryotic Kir channel assembly, in the closed state, refined to a resolution of 3.65 angstroms. We identify the main activation gate and structural elements involved in gating. On the basis of structural evidence presented here, we suggest that gating involves coupling between the intracellular and membrane domains. This further suggests that initiation of gating by membrane or intracellular signals represents different entry points to a common mechanistic pathway.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amino Acid Sequence
  • Bacterial Proteins / chemistry*
  • Bacterial Proteins / metabolism
  • Binding Sites
  • Burkholderia pseudomallei / chemistry*
  • Crystallization
  • Crystallography, X-Ray
  • Dimerization
  • Hydrophobic and Hydrophilic Interactions
  • Ion Channel Gating*
  • Ion Transport
  • Models, Molecular
  • Molecular Sequence Data
  • Potassium / metabolism
  • Potassium Channels, Inwardly Rectifying / chemistry*
  • Potassium Channels, Inwardly Rectifying / metabolism
  • Protein Conformation
  • Protein Structure, Quaternary
  • Protein Structure, Secondary
  • Protein Structure, Tertiary

Substances

  • Bacterial Proteins
  • Potassium Channels, Inwardly Rectifying
  • Potassium

Associated data

  • PDB/1P7B