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Backbone and Sidechain 1H, 15N and 13C Resonance Assignments of a Multidrug Efflux Membrane Protein using Solution and Solid-State NMR

Harding, B. D.; Hiett, A. B.; Tonelli, M.; Wang, S.; Rienstra, C. M.; Henzler-Wildman, K. A.

2025-01-10 biophysics
10.1101/2025.01.07.631770 bioRxiv
Show 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.

Published in Biomolecular NMR Assignments · not in our set (fewer than 10 published preprints to learn from) · training set

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