Detecting Substrates Bound to the Secondary Multidrug Efflux Pump EmrE by DNP-Enhanced Solid-State NMR
Author:
Affiliation:
1. Institute of Biophysical Chemistry & Centre for Biomolecular Magnetic Resonance and ‡Institute of Biochemistry, Goethe University Frankfurt, Max-von-Laue-Str. 9, 60438 Frankfurt am Main, Germany
Publisher
American Chemical Society (ACS)
Subject
Colloid and Surface Chemistry,Biochemistry,General Chemistry,Catalysis
Link
https://pubs.acs.org/doi/pdf/10.1021/ja402605s
Reference44 articles.
1. EmrE, an Escherichia coli 12-kDa Multidrug Transporter, Exchanges Toxic Cations and H+ and Is Soluble in Organic Solvents
2. A membrane-embedded glutamate is required for ligand binding to the multidrug transporter EmrE
3. In Vitro Monomer Swapping in EmrE, a Multidrug Transporter from Escherichia coli, Reveals That the Oligomer Is the Functional Unit
4. Parallel topology of genetically fused EmrE homodimers
5. Conformational Changes in the Multidrug Transporter EmrE Associated with Substrate Binding
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