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<p>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 <sup>1</sup>H, <sup>15</sup>N, and <sup>13</sup>C 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 <sup>13</sup>C-detected experiments in liposomes.</p>

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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

  • 期刊论文

  • 出版模式：

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  • 发表日期：

    2025年5月27日

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

摘要

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.