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

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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 2H13C15N 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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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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Authors and Affiliations

  1. Chemistry Department, College of Staten Island, 2800 Victory Boulevard, Staten Island, NY, 10314, USA

    Sébastien F. Poget

  2. Biochemistry Department, Albert Einstein College of Medicine, 1300 Morris Park Ave, Bronx, NY, 10461, USA

    Richard Harris, Sean M. Cahill & Mark E. Girvin

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  1. Sébastien F. Poget
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  2. Richard Harris
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  3. Sean M. Cahill
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  4. Mark E. Girvin
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Correspondence to Mark E. Girvin.

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Poget, S.F., Harris, R., Cahill, S.M. et al. 1H, 13C, 15N backbone NMR assignments of the Staphylococcus aureus small multidrug-resistance pump (Smr) in a functionally active conformation. Biomol NMR Assign 4, 139–142 (2010). https://doi.org/10.1007/s12104-010-9228-7

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  • DOI: https://doi.org/10.1007/s12104-010-9228-7

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