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

Sébastien F. Poget; Richard Harris; Sean M. Cahill; Mark E. Girvin

doi:10.1007/s12104-010-9228-7

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

Sébastien F. Poget, Richard Harris, Sean M. Cahill, Mark E. Girvin

Biochemistry

Research output: Contribution to journal › Article › peer-review

13 Scopus citations

Abstract

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)
Pages (from-to)	139-142
Number of pages	4
Journal	Biomolecular NMR Assignments
Volume	4
Issue number	2
DOIs	https://doi.org/10.1007/s12104-010-9228-7
State	Published - Oct 2010

Keywords

Bicelle
MDR
Membrane protein
NMR
Smr

ASJC Scopus subject areas

Structural Biology
Biochemistry

Access to Document

10.1007/s12104-010-9228-7

Cite this

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

abstract = "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.",

keywords = "Bicelle, MDR, Membrane protein, NMR, Smr",

author = "Poget, {S{\'e}bastien F.} and Richard Harris and Cahill, {Sean M.} and Girvin, {Mark E.}",

note = "Funding Information: Acknowledgments This work was supported by NIH grant GM072085. Many of the NMR experiments were performed at the New York Structural Biology Center, which is a STAR center supported by the New York State Office of Science, Technology, and Academic Research; its 900 MHz spectrometers were purchased with funds from NIH, USA, the Keck Foundation, New York State, and the NYC Economic Development Corporation.",

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AU - Poget, Sébastien F.

AU - Harris, Richard

AU - Cahill, Sean M.

AU - Girvin, Mark E.

N1 - Funding Information: Acknowledgments This work was supported by NIH grant GM072085. Many of the NMR experiments were performed at the New York Structural Biology Center, which is a STAR center supported by the New York State Office of Science, Technology, and Academic Research; its 900 MHz spectrometers were purchased with funds from NIH, USA, the Keck Foundation, New York State, and the NYC Economic Development Corporation.

PY - 2010/10

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N2 - 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.

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