1H, 13C, 15N backbone NMR assignments of the Staphylococcus aureus small multidrug-resistance pump (Smr) in a functionally active conformation.
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 (2)H(13)C(15)N 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.
Poget
Sébastien F
SF
Chemistry Department, College of Staten Island, 2800 Victory Boulevard, Staten Island, NY 10314, USA.
Harris
Richard
R
Cahill
Sean M
SM
Girvin
Mark E
ME
D017920:Antiporters / Q000737:chemistry*; D002247:Carbon Isotopes; D006859:Hydrogen; D009587:Nitrogen Isotopes; D019906:Nuclear Magnetic Resonance, Biomolecular; D017433:Protein Structure, Secondary; D013211:Staphylococcus aureus / Q000737:chemistry*
D017920:Antiporters; D002247:Carbon Isotopes; D009587:Nitrogen Isotopes; C521590:small multidrug-resistance pump, Staphylococcus aureus; D006859:Hydrogen
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