Backbone and Sidechain¹H,¹⁵N and¹³C Resonance Assignments of a Multidrug Efflux Membrane Protein using Solution and Solid-State NMR

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 includes¹H,¹⁵N, and¹³C 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 NMR¹³C-detected experiments in liposomes.