Studying the active-site loop movement of the São Paolo metallo-β-lactamase-1
Author:
Affiliation:
1. Department of Chemistry
2. University of Oxford
3. Oxford
4. UK
5. Physical and Theoretical Chemistry Laboratory
6. School of Cellular and Molecular Medicine
7. University of Bristol
8. Bristol
Abstract
A unique structural and biophysical characterization using crystallographic, native ion-mobility mass spectrometry and 19F NMR identifies movement of a loop as being important in SPM-1 catalysis.
Publisher
Royal Society of Chemistry (RSC)
Subject
General Chemistry
Link
http://pubs.rsc.org/en/content/articlepdf/2015/SC/C4SC01752H
Reference39 articles.
1. A 1.2-A snapshot of the final step of bacterial cell wall biosynthesis
2. Metallo-β-Lactamases: the Quiet before the Storm?
3. Updated Functional Classification of β-Lactamases
4. International gatherings and potential for global dissemination of São Paulo metallo-β-lactamase (SPM) from Brazil
5. First Report of the Metallo-β-Lactamase SPM-1 in Europe
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