Emulating Membrane Protein Evolution by Rational Design
- 2 March 2007
- journal article
- other
- Published by American Association for the Advancement of Science (AAAS) in Science
- Vol. 315 (5816), 1282-1284
- https://doi.org/10.1126/science.1135406
Abstract
How do integral membrane proteins evolve in size and complexity? Using the small multidrug-resistance protein EmrE from Escherichia coli as a model, we experimentally demonstrated that the evolution of membrane proteins composed of two homologous but oppositely oriented domains can occur in a small number of steps: An original dual-topology protein evolves, through a gene-duplication event, to a heterodimer formed by two oppositely oriented monomers. This simple evolutionary pathway can explain the frequent occurrence of membrane proteins with an internal pseudo–two-fold symmetry axis in the plane of the membrane.Keywords
This publication has 27 references indexed in Scilit:
- Structure of a bacterial multidrug ABC transporterNature, 2006
- Structure of the Multidrug Transporter EmrD from Escherichia coliScience, 2006
- Crystal structure of a bacterial homologue of Na+/Cl--dependent neurotransmitter transportersNature, 2005
- Internal Gene Duplication in the Evolution of Prokaryotic Transmembrane ProteinsJournal of Molecular Biology, 2004
- X-ray structure of a protein-conducting channelNature, 2003
- Structure of mitochondrial ADP/ATP carrier in complex with carboxyatractylosideNature, 2003
- Structure and Mechanism of the Lactose Permease of Escherichia coliScience, 2003
- Structure and Mechanism of the Glycerol-3-Phosphate Transporter from Escherichia coliScience, 2003
- Crystal structure of bacterial multidrug efflux transporter AcrBNature, 2002
- The E. coli BtuCD Structure: A Framework for ABC Transporter Architecture and MechanismScience, 2002