Difference: PogetCahill07 (4 vs. 5)
Revision 513 Mar 2007 - Main.JasperShahn
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| Although detergent micelles are commonly used as membrane mimetics in biophysical studies of membrane proteins, they do not ideally reproduce the native environment of the protein in the membrane and may fail to support the native fold of the protein. Not surprisingly, these nonphysiological conformations are particularly common for helical membrane proteins that undergo significant conformational changes as part of their functional cycle, such as the voltage sensor domain of potassium channels, G-proteincoupled receptors, and bacterial multidrug transporters. One dramatic example is the small multidrug-resistance pump EmrE from Escherichia coli, which was found in three significantly different conformations in two X-ray structures in detergent1,2 and a cryo-electron microscopy 3D reconstruction map from 2D crystals.3 The functional relevance of these structures is the subject of current debate,4 and an alternative method of getting highresolution structural information about the functional protein is certainly needed. Bicelles, which are a mixture of short- and longchain lipids, have long been suggested as a more native-like solubilizing agent for the study of membrane proteins,5-7 and have been used in a number of biophysical and structural studies of these proteins (for a recent review, see ref 8). Here we show that bicelles are a promising system in the study of Smr, the EmrE homologue from Staphylococcus aureus, since they both preserve the ligandbinding activity and produce NMR spectra that allowed making substantial NMR backbone assignments for this conformationally flexible protein. | ||||||||
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