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

Research output: Contribution to journalArticle

10 Scopus citations


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 languageEnglish (US)
Pages (from-to)139-142
Number of pages4
JournalBiomolecular NMR Assignments
Issue number2
Publication statusPublished - Oct 1 2010



  • Bicelle
  • MDR
  • Membrane protein
  • NMR
  • Smr

ASJC Scopus subject areas

  • Structural Biology
  • Biochemistry

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