The plasmid-encoded small multidrug resistance pump from S. aureus transports a variety of quaternary ammonium and other hydrophobic compounds, enhancing the bacterial host's resistance to common hospital disinfectants. The protein folds as a homo-dimer of four transmembrane helices each, and appears to be fully functional only in lipid bilayers. Here we report the backbone resonance assignments and implied secondary structure for 2H 13C15N Smr reconstituted into lipid bicelles. Significant changes were observed between the chemical shifts of the protein in lipid bicelles compared to those in detergent micelles.
|Original language||English (US)|
|Number of pages||4|
|Journal||Biomolecular NMR Assignments|
|State||Published - Oct 2010|
- Membrane protein
ASJC Scopus subject areas
- Structural Biology