1H, 13C, 15N backbone NMR assignments of the Staphylococcus aureus small multidrug-resistance pump (Smr) in a functionally active conformation

被引：12
|
作者：
Poget, Sebastien F. [2 ]
Harris, Richard [1 ]
Cahill, Sean M. [1 ]
Girvin, Mark E. [1 ]
机构：
[1] Albert Einstein Coll Med, Dept Biochem, Bronx, NY 10461 USA
[2] CUNY Coll Staten Isl, Dept Chem, Staten Isl, NY 10314 USA
来源：
BIOMOLECULAR NMR ASSIGNMENTS | 2010年 / 4卷 / 02期
关键词：
MDR; Smr; NMR; Bicelle; Membrane protein; TRANSPORTER EMRE; MEMBRANE-PROTEIN; MODEL; EVOLUTION; TOPOLOGY;
D O I：
10.1007/s12104-010-9228-7
中图分类号：
Q6 [生物物理学];
学科分类号：
071011 ;
摘要：
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 (HCN)-H-2-C-13-N-15 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.
引用
收藏
页码：139 / 142
页数：4
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