[NMR paper] Backbone NMR assignment of the nucleotide binding domain of the Bacillus subtilis ABC multidrug transporter BmrA in the post-hydrolysis state
Backbone NMR assignment of the nucleotide binding domain of the Bacillus subtilis ABC multidrug transporter BmrA in the post-hydrolysis state
ATP binding cassette (ABC) proteins are present in all phyla of life and form one of the largest protein families. The Bacillus subtilis ABC transporter BmrA is a functional homodimer that can extrude many different harmful compounds out of the cell. Each BmrA monomer is composed of a transmembrane domain (TMD) and a nucleotide binding domain (NBD). While the TMDs of ABC transporters are sequentially diverse, the highly conserved NBDs harbor...
[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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01-15-2014 05:16 PM
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...
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08-14-2013 05:24 PM
[NMR paper] Amino acid type selective isotope labelling of the multidrug ABC transporter LmrA for
Amino acid type selective isotope labelling of the multidrug ABC transporter LmrA for solid-state NMR studies.
Related Articles Amino acid type selective isotope labelling of the multidrug ABC transporter LmrA for solid-state NMR studies.
FEBS Lett. 2004 Jun 18;568(1-3):117-21
Authors: Mason AJ, Siarheyeva A, Haase W, Lorch M, van Veen H, Glaubitz C
The ABC transporter LmrA in Lactococcus lactis confers resistance to a wide range of antibiotics and cytotoxic drugs and is a functional homologue of P-glycoprotein. Recently, solid-state NMR...
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[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...