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Ligand‐Induced Conformational Changes of the Multidrug Resistance Transporter EmrE Probed by Oriented Solid‐State NMR Spectroscopy
Author(s) -
Gayen Anindita,
Banigan James R.,
Traaseth Nathaniel J.
Publication year - 2013
Publication title -
angewandte chemie international edition
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 5.831
H-Index - 550
eISSN - 1521-3773
pISSN - 1433-7851
DOI - 10.1002/anie.201303091
Subject(s) - nuclear magnetic resonance spectroscopy , lipid bilayer , chemistry , transporter , ligand (biochemistry) , solid state nuclear magnetic resonance , conformational change , crystallography , biophysics , monomer , spectroscopy , membrane protein , membrane , stereochemistry , nuclear magnetic resonance , biochemistry , biology , receptor , polymer , organic chemistry , physics , quantum mechanics , gene
An EmrE‐ging market : Oriented solid‐state NMR spectroscopy and biochemical cross‐linking experiments were used to show that the ligand‐free membrane protein transporter EmrE forms anti‐parallel dimers with different monomer tilt angles relative to the lipid bilayer. In addition, subtle conformational changes were detected upon drug binding that emphasize the need for an atomic‐resolution structure.