Ligand-induced conformational changes of the multidrug resistance transporter EmrE probed by oriented solid-state NMR spectroscopy.
Department of Chemistry, New York University, 100 Washington Square East, New York, NY 10003 (USA) http://www.nyu.edu/fas/dept/chemistry/traasethgroup/
Anindita
A
Gayen
James R
JR
Banigan
Nathaniel J
NJ
Traaseth
D000595:Amino Acid Sequence; D017920:Antiporters / Q000737:chemistry* / Q000378:metabolism; D024901:Drug Resistance, Multiple, Bacterial; D004926:Escherichia coli / Q000737:chemistry* / Q000187:drug effects / Q000378:metabolism; D029968:Escherichia coli Proteins / Q000737:chemistry* / Q000378:metabolism; D008024:Ligands; D008958:Models, Molecular; D008969:Molecular Sequence Data; D019906:Nuclear Magnetic Resonance, Biomolecular; D011487:Protein Conformation / Q000187:drug effects; D055503:Protein Multimerization
D017920:Antiporters; D029968:Escherichia coli Proteins; D008024:Ligands; C075436:EmrE protein, E coli
EmrE; NMR spectroscopy; membrane proteins; multidrug resistance; oriented solid-state NMR