Quasi-symmetry in the Cryo-EM Structure of EmrE Provides the Key to Modeling its Transmembrane Domain
- 1 November 2006
- journal article
- Published by Elsevier in Journal of Molecular Biology
- Vol. 364 (1) , 54-67
- https://doi.org/10.1016/j.jmb.2006.08.072
Abstract
No abstract availableKeywords
This publication has 58 references indexed in Scilit:
- Identification and evolution of dual-topology membrane proteinsNature Structural & Molecular Biology, 2006
- The Escherichia coli Multidrug Transporter EmrE is a Dimer in the Detergent-solubilised StateJournal of Molecular Biology, 2004
- The membrane topology of EmrE – a small multidrug transporter from Escherichia coliFEBS Letters, 2004
- New insights into the structure and oligomeric state of the bacterial multidrug transporter EmrE: an unusual asymmetric homo‐dimerFEBS Letters, 2004
- X-ray structure of a protein-conducting channelNature, 2003
- Structure and Mechanism of the Lactose Permease of Escherichia coliScience, 2003
- Structural Biology of Bacterial Multidrug Resistance Gene RegulatorsPublished by Elsevier ,2002
- A Novel Scoring Function for Predicting the Conformations of Tightly Packed Pairs of Transmembrane α-HelicesJournal of Molecular Biology, 2002
- An alpha-carbon template for the transmembrane helices in the rhodopsin family of G-protein-coupled receptors 1 1Edited by R. HuberJournal of Molecular Biology, 1997
- CLUSTAL W: improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position-specific gap penalties and weight matrix choiceNucleic Acids Research, 1994