Abstract
An EmrE-ging market: Oriented solid-state NMR spectroscopy and biochemical cross-linking experiments were used to show that the ligand-free membrane protein transporter EmrE forms anti-parallel dimers with different monomer tilt angles relative to the lipid bilayer. In addition, subtle conformational changes were detected upon drug binding that emphasize the need for an atomic-resolution structure.
| Original language | English (US) |
|---|---|
| Pages (from-to) | 10321-10324 |
| Number of pages | 4 |
| Journal | Angewandte Chemie - International Edition |
| Volume | 52 |
| Issue number | 39 |
| DOIs | |
| State | Published - Sep 23 2013 |
Keywords
- EmrE
- NMR spectroscopy
- membrane proteins
- multidrug resistance
- oriented solid-state NMR
ASJC Scopus subject areas
- Catalysis
- Chemistry(all)
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Gayen, A., Banigan, J. R., & Traaseth, N. J. (2013). Ligand-induced conformational changes of the multidrug resistance transporter EmrE probed by oriented solid-state NMR spectroscopy. Angewandte Chemie - International Edition, 52(39), 10321-10324. https://doi.org/10.1002/anie.201303091