Ligand-induced conformational changes of the multidrug resistance transporter EmrE probed by oriented solid-state NMR spectroscopy

Anindita Gayen, James R. Banigan, Nathaniel Traaseth

Research output: Contribution to journalArticle

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 languageEnglish (US)
Pages (from-to)10321-10324
Number of pages4
JournalAngewandte Chemie - International Edition
Volume52
Issue number39
DOIs
StatePublished - Sep 23 2013

Fingerprint

Lipid bilayers
Dimers
Nuclear magnetic resonance spectroscopy
Membrane Proteins
Monomers
Ligands
Proteins
Membranes
Pharmaceutical Preparations
Experiments

Keywords

  • EmrE
  • membrane proteins
  • multidrug resistance
  • NMR spectroscopy
  • oriented solid-state NMR

ASJC Scopus subject areas

  • Chemistry(all)
  • Catalysis

Cite this

Ligand-induced conformational changes of the multidrug resistance transporter EmrE probed by oriented solid-state NMR spectroscopy. / Gayen, Anindita; Banigan, James R.; Traaseth, Nathaniel.

In: Angewandte Chemie - International Edition, Vol. 52, No. 39, 23.09.2013, p. 10321-10324.

Research output: Contribution to journalArticle

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