NMR Spectroscopy Approach to Study the Structure, Orientation, and Mechanism of the Multidrug Exporter EmrE.
Methods Mol Biol. 2018;1700:83-96
Authors: Leninger M, Traaseth NJ
Abstract
Multidrug exporters are a class of membrane proteins that remove antibiotics from the cytoplasm of bacteria and in the process confer multidrug resistance to the organism. This chapter outlines the sample preparation and optimization of oriented solid-state NMR experiments applied to the study of structure and dynamics for the model transporter EmrE from the small multidrug resistance (SMR) family.
[NMR paper] Detecting substrates bound to the secondary multidrug efflux pump EmrE by DNP-enhanced solid-state NMR.
Detecting substrates bound to the secondary multidrug efflux pump EmrE by DNP-enhanced solid-state NMR.
http://www.bionmr.com//www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--pubs.acs.org-images-pubmed-acspubs.jpg Related Articles Detecting substrates bound to the secondary multidrug efflux pump EmrE by DNP-enhanced solid-state NMR.
J Am Chem Soc. 2013 Oct 23;135(42):15754-62
Authors: Ong YS, Lakatos A, Becker-Baldus J, Pos KM, Glaubitz C
Abstract
Escherichia coli EmrE, a homodimeric multidrug antiporter, has been suggested to...
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Detecting substrates bound to the secondary multidrug efflux pump EmrE by DNP-enhanced solid-state NMR
From The DNP-NMR Blog:
Detecting substrates bound to the secondary multidrug efflux pump EmrE by DNP-enhanced solid-state NMR
Ong, Y.S., et al., Detecting substrates bound to the secondary multidrug efflux pump EmrE by DNP-enhanced solid-state NMR. J Am Chem Soc, 2013. 135(42): p. 15754-62.
http://www.ncbi.nlm.nih.gov/pubmed/24047229
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Detecting Substrates Bound to the Secondary Multidrug Efflux Pump EmrE by DNP-Enhanced Solid-State NMR
Detecting Substrates Bound to the Secondary Multidrug Efflux Pump EmrE by DNP-Enhanced Solid-State NMR
Yean Sin Ong, Andrea Lakatos, Johanna Becker-Baldus, Klaas M. Pos and Clemens Glaubitz
http://pubs.acs.org/appl/literatum/publisher/achs/journals/content/jacsat/0/jacsat.ahead-of-print/ja402605s/aop/images/medium/ja-2013-02605s_0006.gif
Journal of the American Chemical Society
DOI: 10.1021/ja402605s
http://feeds.feedburner.com/~ff/acs/jacsat?d=yIl2AUoC8zA
http://feeds.feedburner.com/~r/acs/jacsat/~4/AjOxCwRFsQs
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10-12-2013 12:59 AM
[NMR paper] Ligand-Induced Conformational Changes of the Multidrug Resistance Transporter EmrE Probed by Oriented Solid-State NMR Spectroscopy.
Ligand-Induced Conformational Changes of the Multidrug Resistance Transporter EmrE Probed by Oriented Solid-State NMR Spectroscopy.
Ligand-Induced Conformational Changes of the Multidrug Resistance Transporter EmrE Probed by Oriented Solid-State NMR Spectroscopy.
Angew Chem Int Ed Engl. 2013 Aug 12;
Authors: Gayen A, Banigan JR, Traaseth NJ
Abstract
An EmrE-ging market: Oriented solid-state NMR spectroscopy and biochemical cross-linking experiments were used to show that the ligand-free membrane protein transporter EmrE forms...
[NMR paper] NMR investigation of the multidrug transporter EmrE, an integral membrane protein.
NMR investigation of the multidrug transporter EmrE, an integral membrane protein.
Related Articles NMR investigation of the multidrug transporter EmrE, an integral membrane protein.
Eur J Biochem. 1998 Jun 15;254(3):610-9
Authors: Schwaiger M, Lebendiker M, Yerushalmi H, Coles M, Gröger A, Schwarz C, Schuldiner S, Kessler H
EmrE is an Escherichia coli multidrug transport protein that confers resistance to a wide range of toxicants by active transport across the bacterial cell membrane. The highly hydrophobic polytopic integral membrane...
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[NMR paper] 31P and 13C NMR spectroscopic study of wild type and multidrug resistant Ehrlich asci
31P and 13C NMR spectroscopic study of wild type and multidrug resistant Ehrlich ascites tumor cells.
Related Articles 31P and 13C NMR spectroscopic study of wild type and multidrug resistant Ehrlich ascites tumor cells.
Oncol Res. 1993;5(3):119-26
Authors: Rasmussen J, Hansen LL, Friche E, Jaroszewski JW
Steady-state 31P NMR spectra of wild type EHR2 Ehrlich ascites tumor cells and multidrug resistant EHR2/DNR+ cells, immobilized in agarose threads, and continuously perfused with medium, showed temperature-dependent differences in the levels...
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08-21-2010 11:53 PM
[NMR paper] 1H-NMR study of the mechanism of assembly and equilibrium heme orientation of sperm w
1H-NMR study of the mechanism of assembly and equilibrium heme orientation of sperm whale myoglobin reconstituted with protohemin type-isomers.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--linkinghub.elsevier.com-ihub-images-PubMedLink.gif Related Articles 1H-NMR study of the mechanism of assembly and equilibrium heme orientation of sperm whale myoglobin reconstituted with protohemin type-isomers.
Biochim Biophys Acta. 1990 Nov 15;1041(2):186-94
Authors: Hauksson JB, La Mar GN, Pande U, Pandey RK, Parish DW, Singh JP, Smith KM
The...