The Escherichia coli Multidrug Transporter EmrE is a Dimer in the Detergent-solubilised State
- 16 July 2004
- journal article
- Published by Elsevier in Journal of Molecular Biology
- Vol. 340 (4) , 797-808
- https://doi.org/10.1016/j.jmb.2004.05.014
Abstract
No abstract availableKeywords
This publication has 34 references indexed in Scilit:
- New insights into the structure and oligomeric state of the bacterial multidrug transporter EmrE: an unusual asymmetric homo‐dimerFEBS Letters, 2004
- Conformational Changes in the Multidrug Transporter EmrE Associated with Substrate BindingJournal of Molecular Biology, 2003
- Crosslinking of membrane-embedded cysteines reveals contact points in the EmrE oligomerProceedings of the National Academy of Sciences, 2002
- In Vitro Monomer Swapping in EmrE, a Multidrug Transporter from Escherichia coli, Reveals That the Oligomer Is the Functional UnitPublished by Elsevier ,2001
- A Model for Coupling of H+ and Substrate Fluxes Based on “Time-Sharing” of a Common Binding SiteBiochemistry, 2000
- A membrane-embedded glutamate is required for ligand binding to the multidrug transporter EmrEThe EMBO Journal, 2000
- Negative Dominance Studies Demonstrate the Oligomeric Structure of EmrE, a Multidrug Antiporter from Escherichia coliJournal of Biological Chemistry, 1996
- The SMR family: a novel family of multidrug efflux proteins involved with the efflux of lipophilic drugsMolecular Microbiology, 1996
- Determining the Secondary Structure and Orientation of EmrE, a Multi-Drug Transporter, Indicates a Transmembrane Four-Helix BundleBiochemistry, 1996
- EmrE, an Escherichia coli 12-kDa Multidrug Transporter, Exchanges Toxic Cations and H+ and Is Soluble in Organic SolventsJournal of Biological Chemistry, 1995