Solid-state NMR study and assignments of the KcsA potassium ion channel of S. lividans.
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.
Varga
Krisztina
K
Department of Chemistry, Columbia University, 3000 Broadway MC 3113, New York, NY 10027, USA.
Tian
Lin
L
McDermott
Ann E
AE
D000595:Amino Acid Sequence; D001426:Bacterial Proteins / Q000737:chemistry*; D002247:Carbon Isotopes / Q000737:chemistry; D009682:Magnetic Resonance Spectroscopy; D008969:Molecular Sequence Data; D015221:Potassium Channels / Q000737:chemistry*; D017433:Protein Structure, Secondary; D048170:Streptomyces lividans / Q000737:chemistry
D001426:Bacterial Proteins; D002247:Carbon Isotopes; D015221:Potassium Channels; C107790:prokaryotic potassium channel