[NMR paper] Revealing Cell-Surface Intramolecular Interactions in the BlaR1 Protein of Methicillin-Resistant Staphylococcus aureus by NMR Spectroscopy.
Related ArticlesRevealing Cell-Surface Intramolecular Interactions in the BlaR1 Protein of Methicillin-Resistant Staphylococcus aureus by NMR Spectroscopy.
Biochemistry. 2013 Dec 20;
Authors: Frederick TE, Wilson BD, Cha J, Mobashery S, Peng JW
Abstract
In methicillin-resistant Staphylococcus aureus, ?-lactam antibiotic resistance is mediated by the transmembrane protein BlaR1. The antibiotic-sensor domain BlaRS and the L2 loop of BlaR1 are on the membrane surface. We used NMR to investigate interactions between BlaRS and a wa-ter-soluble peptide from L2. This peptide binds BlaRS proximal to the antibiotic acylation site as an amphipathic helix. BlaRS acylation by penicillin G does not disrupt binding. These results suggest a signal transduction mechanism whereby the L2 helix, partially embedded in the membrane, propagates conformational changes caused by BlaRS acylation through the membrane via transmembrane segments, leading to antibiotic resistance.
PMID: 24359467 [PubMed - as supplied by publisher]
[NMR paper] (1)H, (13)C, (15)N backbone and side chain NMR resonance assignments of the N-terminal NEAr iron transporter domain 1 (NEAT 1) of the hemoglobin receptor IsdB of Staphylococcus aureus.
(1)H, (13)C, (15)N backbone and side chain NMR resonance assignments of the N-terminal NEAr iron transporter domain 1 (NEAT 1) of the hemoglobin receptor IsdB of Staphylococcus aureus.
Related Articles (1)H, (13)C, (15)N backbone and side chain NMR resonance assignments of the N-terminal NEAr iron transporter domain 1 (NEAT 1) of the hemoglobin receptor IsdB of Staphylococcus aureus.
Biomol NMR Assign. 2013 May 18;
Authors: Fonner BA, Tripet BP, Lui M, Zhu H, Lei B, Copié V
Abstract
Staphylococcus aureus is an opportunistic pathogen that...
Exploring weak, transient protein-protein interactions in crowded in vivo environments by in-cell NMR spectroscopy.
Exploring weak, transient protein-protein interactions in crowded in vivo environments by in-cell NMR spectroscopy.
Exploring weak, transient protein-protein interactions in crowded in vivo environments by in-cell NMR spectroscopy.
Biochemistry. 2011 Sep 26;
Authors: Wang Q, Zhuravleva A, Gierasch LM
Abstract
Biology relies on functional interplay of proteins in the crowded and heterogeneous environment inside cells, and functional protein interactions are often weak and transient. Thus, methods are needed that preserve these interactions...
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09-30-2011 06:00 AM
Exploring weak, transient protein-protein interactions in crowded in vivo environments by in-cell NMR spectroscopy.
Exploring weak, transient protein-protein interactions in crowded in vivo environments by in-cell NMR spectroscopy.
Exploring weak, transient protein-protein interactions in crowded in vivo environments by in-cell NMR spectroscopy.
Biochemistry. 2011 Sep 26;
Authors: Wang Q, Zhuravleva A, Gierasch LM
Abstract
Biology relies on functional interplay of proteins in the crowded and heterogeneous environment inside cells, and functional protein interactions are often weak and transient. Thus, methods are needed that preserve these...
nmrlearner
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0
09-30-2011 05:59 AM
Protein Interactions in the Escherichia coli Cytosol: An Impediment to In-Cell NMR Spectroscopy.
Protein Interactions in the Escherichia coli Cytosol: An Impediment to In-Cell NMR Spectroscopy.
Protein Interactions in the Escherichia coli Cytosol: An Impediment to In-Cell NMR Spectroscopy.
Chembiochem. 2011 Mar 29;
Authors: Crowley PB, Chow E, Papkovskaia T
Protein science is shifting towards experiments performed under native or native-like conditions. In-cell NMR spectroscopy for instance has the potential to reveal protein structure and dynamics inside cells. However, not all proteins can be studied by this technique. (15) N-labelled...
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03-31-2011 06:24 PM
[NMR paper] Identification of residues involved in the interaction of Staphylococcus aureus fibro
Identification of residues involved in the interaction of Staphylococcus aureus fibronectin-binding protein with the (4)F1(5)F1 module pair of human fibronectin using heteronuclear NMR spectroscopy.
Related Articles Identification of residues involved in the interaction of Staphylococcus aureus fibronectin-binding protein with the (4)F1(5)F1 module pair of human fibronectin using heteronuclear NMR spectroscopy.
Biochemistry. 2000 Mar 21;39(11):2887-93
Authors: Penkett CJ, Dobson CM, Smith LJ, Bright JR, Pickford AR, Campbell ID, Potts JR
Many...
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11-18-2010 09:15 PM
[NMR paper] Two-dimensional 1H NMR studies on HPr protein from Staphylococcus aureus: complete se
Two-dimensional 1H NMR studies on HPr protein from Staphylococcus aureus: complete sequential assignments and secondary structure.
Related Articles Two-dimensional 1H NMR studies on HPr protein from Staphylococcus aureus: complete sequential assignments and secondary structure.
Biochemistry. 1991 Nov 19;30(46):11186-92
Authors: Kalbitzer HR, Neidig KP, Hengstenberg W
Complete sequence-specific assignments of the 1H NMR spectrum of HPr protein from Staphylococcus aureus were obtained by two-dimensional NMR methods. Important secondary structure...
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08-21-2010 11:12 PM
[NMR paper] Two-dimensional 1H NMR studies on HPr protein from Staphylococcus aureus: complete se
Two-dimensional 1H NMR studies on HPr protein from Staphylococcus aureus: complete sequential assignments and secondary structure.
Related Articles Two-dimensional 1H NMR studies on HPr protein from Staphylococcus aureus: complete sequential assignments and secondary structure.
Biochemistry. 1991 Nov 19;30(46):11186-92
Authors: Kalbitzer HR, Neidig KP, Hengstenberg W
Complete sequence-specific assignments of the 1H NMR spectrum of HPr protein from Staphylococcus aureus were obtained by two-dimensional NMR methods. Important secondary structure...
Revealing Cell-Surface Intramolecular Interactions in the BlaR1 Protein of Methicillin-Resistant Staphylococcus aureus by NMR Spectroscopy.
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