title: MAS solid-state NMR studies on the multidrug transporter EmrE.
abstract: We study the uniformly 13C,15N isotopically enriched Escherichia coli multidrug resistance transporter EmrE using MAS solid-state NMR. Solid-state NMR can provide complementary structural information as the method allows studying membrane proteins in their native environment as no detergent is required for reconstitution. We compare the spectra obtained from wildtype EmrE to those obtained from the mutant EmrE-E14C. To resolve the critical amino acid E14, glutamic/aspartic acid selective experiments are carried out. These experiments allow to assign the chemical shift of the carboxylic carbon of E14. In addition, spectra are analyzed which are obtained in the presence and absence of the ligand TPP+.
authors.affiliation: Leibniz-Institut für Molekulare Pharmakologie (FMP), Robert-Rössle-Str. 10, D-13125 Berlin, Germany.
authors.forename: Vipin
authors.initials: V
authors.lastname: Agarwal
authors.forename: Uwe
authors.initials: U
authors.lastname: Fink
authors.forename: Shimon
authors.initials: S
authors.lastname: Schuldiner
authors.forename: Bernd
authors.initials: B
authors.lastname: Reif
mesh_terms: D017920:Antiporters / Q000737:chemistry* / Q000648:ultrastructure; D002247:Carbon Isotopes; D029968:Escherichia coli Proteins / Q000737:chemistry* / Q000648:ultrastructure; D009682:Magnetic Resonance Spectroscopy / Q000379:methods*; D008565:Membrane Proteins / Q000737:chemistry / Q000235:genetics / Q000378:metabolism; D008854:Microscopy, Electron; D009154:Mutation; D009587:Nitrogen Isotopes; D009861:Onium Compounds / Q000378:metabolism; D009943:Organophosphorus Compounds / Q000378:metabolism; D011485:Protein Binding
chemical_list: D017920:Antiporters; D002247:Carbon Isotopes; D029968:Escherichia coli Proteins; D008565:Membrane Proteins; D009587:Nitrogen Isotopes; D009861:Onium Compounds; D009943:Organophosphorus Compounds; C075436:EmrE protein, E coli; C013289:tetraphenylphosphonium