title: Solid-state NMR study and assignments of the KcsA potassium ion channel of S. lividans.
abstract: 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.affiliation: Department of Chemistry, Columbia University, 3000 Broadway MC 3113, New York, NY 10027, USA.
authors.forename: Krisztina
authors.initials: K
authors.lastname: Varga
authors.forename: Lin
authors.initials: L
authors.lastname: Tian
authors.forename: Ann E
authors.initials: AE
authors.lastname: McDermott
mesh_terms: 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
chemical_list: D001426:Bacterial Proteins; D002247:Carbon Isotopes; D015221:Potassium Channels; C107790:prokaryotic potassium channel