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 Citations (Scopus)

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 languageEnglish (US)
Pages (from-to)139-142
Number of pages4
JournalBiomolecular NMR Assignments
Volume4
Issue number2
DOIs
StatePublished - Oct 2010

Fingerprint

Conformations
Nuclear magnetic resonance
Pumps
Lipids
Lipid bilayers
Disinfectants
Chemical shift
Lipid Bilayers
Micelles
Multiple Drug Resistance
Ammonium Compounds
Detergents
Dimers
Proteins
Plasmids
Staphylococcus aureus small multidrug-resistance pump

Keywords

  • Bicelle
  • MDR
  • Membrane protein
  • NMR
  • Smr

ASJC Scopus subject areas

  • Structural Biology
  • Biochemistry

Cite this

1H, 13C, 15N backbone NMR assignments of the Staphylococcus aureus small multidrug-resistance pump (Smr) in a functionally active conformation. / Poget, Sébastien F.; Harris, Richard; Cahill, Sean M.; Girvin, Mark E.

In: Biomolecular NMR Assignments, Vol. 4, No. 2, 10.2010, p. 139-142.

Research output: Contribution to journalArticle

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