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Updated: Jun 1, 2025

Atomic Scale Structural Studies of Macromolecular Assemblies by Solid-state Nuclear Magnetic Resonance Spectroscopy
Published on: September 17, 2017
Backbone and Sidechain 1H, 15N and 13C Resonance Assignments of a Multidrug Efflux Membrane Protein using Solution
Benjamin D Harding1,2, Ashley Hiett1,2, Marco Tonelli2,3
1Biophysics Graduate Program, University of Wisconsin-Madison, Madison, WI, 53706 USA.
Abstract:
EmrE is a bacterial membrane-embedded multidrug transporter that functions as an asymmetric homodimer. EmrE is implicated in antibiotic resistance, but is now known to confer either resistance or susceptibility depending on the identity of the small molecule substrate. Here, we report both solution- and solid-state NMR assignments of S64V-EmrE at pH 5.8, below the pKa of critical residues E14 and H110. This includes 1H, 15N, and 13C resonance assignments of the backbone, methyl groups (isoleucine, leucine, valine, threonine and alanine) from solution NMR experiments in bicelles, and backbone and side-chain assignments from solid-state NMR 13C-detected experiments in liposomes.
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