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Default Revealing Cell-Surface Intramolecular Interactions in the BlaR1 Protein of Methicillin-Resistant Staphylococcus aureus by NMR Spectroscopy.

Revealing Cell-Surface Intramolecular Interactions in the BlaR1 Protein of Methicillin-Resistant Staphylococcus aureus by NMR Spectroscopy.

Related Articles Revealing 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]



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