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

Anindita Gayen; James R. Banigan; Nathaniel J. Traaseth

doi:10.1002/anie.201303091

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

Anindita Gayen, James R. Banigan, Nathaniel J. Traaseth

Chemistry

Research output: Contribution to journal › Article › peer-review

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	https://doi.org/10.1002/anie.201303091
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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keywords = "EmrE, NMR spectroscopy, membrane proteins, multidrug resistance, oriented solid-state NMR",

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AU - Banigan, James R.

AU - Traaseth, Nathaniel J.

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KW - EmrE

KW - NMR spectroscopy

KW - membrane proteins

KW - multidrug resistance

KW - oriented solid-state NMR

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

Abstract

Keywords

ASJC Scopus subject areas

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