Solid-state NMR study and assignments of the KcsA potassium ion channel of S. lividans.

Academic Article


  • The extraordinary efficiency and selectivity of potassium channels have made them ideal systems for biophysical and functional studies of ion conduction. We carried out solid-state NMR studies of the selectivity filter region of the protein. Partial site-specific assignments of the NMR signals were obtained based on high field multidimensional solid-state NMR spectra of uniformly (13)C, (15)N enriched KcsA potassium channel from Streptomyces lividans. Both backbone and sidechain atoms were assigned for residues V76-D80 and P83-L90, in and near the selectivity filter region of the protein; this region exhibits good dispersion and useful chemical shift fingerprints. This study will enable structure, dynamic and mechanistic studies of ion conduction by NMR.
  • Authors

  • Varga, Krisztina
  • Tian, Lin
  • McDermott, Ann E
  • Status

    Publication Date

  • December 2007
  • Keywords

  • Amino Acid Sequence
  • Bacterial Proteins
  • Carbon Isotopes
  • Magnetic Resonance Spectroscopy
  • Molecular Sequence Data
  • Potassium Channels
  • Protein Structure, Secondary
  • Streptomyces lividans
  • Digital Object Identifier (doi)

    Pubmed Id

  • 17974509
  • Start Page

  • 1604
  • End Page

  • 1613
  • Volume

  • 1774
  • Issue

  • 12