ArticleBiomolecular NMR assignments2010
1H, 13C, 15N backbone NMR assignments of the Staphylococcus aureus small multidrug-resistance pump (Smr) in a functionally active conformation.
Article in Biomolecular NMR assignments, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.
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Who cites it
8 citing papers in PubMed, 18 citations in OpenAlex.
- Functional promiscuity of small multidrug resistance transporters from Staphylococcus aureus, Pseudomonas aeruginosa, and Francisella tularensis.Molecular microbiology · 2024Article
- Efflux Pump Mediated Antimicrobial Resistance by Staphylococci in Health-Related Environments: Challenges and the Quest for Inhibition.Antibiotics (Basel, Switzerland) · 2021Review
- Perplexing new insight into the dynamics of the EmrE transporter.The Journal of general physiology · 2015Article
- Review and phylogenetic analysis of qac genes that reduce susceptibility to quaternary ammonium compounds in Staphylococcus species.European journal of microbiology & immunology · 2015Review
- A structured loop modulates coupling between the substrate-binding and dimerization domains in the multidrug resistance transporter EmrE.The Journal of biological chemistry · 2015Article
- When detergent meets bilayer: birth and coming of age of lipid bicelles.Progress in nuclear magnetic resonance spectroscopy · 2013Review
- The magic of bicelles lights up membrane protein structure.Chemical reviews · 2012Review
- Reconstitution of integral membrane proteins into isotropic bicelles with improved sample stability and expanded lipid composition profile.Biochimica et biophysica acta · 2012Article
Corrections and comments
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Authors and funding
4 authors at 2 institutions in 1 country.
Funding
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 (2)H(13)C(15)N 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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