Work

Backbone and sidechain 1H, 15N and 13C resonance assignments of a multidrug efflux membrane protein using solution and solid-state NMR

Year: 2025

Type: article

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.

Source: Biomolecular NMR Assignments

DOI: 10.1007/s12104-025-10238-1

Authors: Benjamin D. Harding, Ashley Hiett, Marco Tonelli, Songlin Wang, Chad M. Rienstra, Katherine A. Henzler-Wildman

Institution: University of Wisconsin–Madison

Language: English

Topic: Advanced NMR Techniques and Applications

Subfield: Spectroscopy

Field: Chemistry

Domain: Physical Sciences

Open Access status: hybrid

Estimated APC paid: $3,890

Funders: National Science Foundation, University of Wisconsin-Madison, National Institutes of Health, National Institute of General Medical Sciences