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

页码：139 / 142

页数：4

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