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Title: Complete [superscript 1]H, [superscript 15]N and [superscript 13]C resonance assignments of Bacillus cereus metallo-β-lactamase and its complex with the inhibitor R-thiomandelic acid
Authors: Karsisiotis, Andreas Ioannis
Damblon, Christian
Roberts, Gordon C.K.
First Published: 10-Jul-2013
Publisher: Springer Netherlands
Citation: Biomolecular NMR Assignments, 2013, in press
Abstract: β-Lactamases inactivate β-lactam antibiotics by hydrolysis of their endocyclic β-lactam bond and are a major cause of antibiotic resistance in pathogenic bacteria. The zinc dependent metallo- β-lactamase enzymes are of particular concern since they are located on highly transmissible plasmids and have a broad spectrum of activity against almost all β-lactam antibiotics. We present here essentially complete (>96 %) backbone and sidechain sequence-specific NMR resonance assignments for the Bacillus cereus subclass B1 metallo-β-lactamase, BcII, and for its complex with R-thiomandelic acid, a broad spectrum inhibitor of metallo-β-lactamases. These assignments have been used as the basis for determination of the solution structures of the enzyme and its inhibitor complex and can also be used in a rapid screen for other metallo-β-lactamase inhibitors.
DOI Link: 10.1007/s12104-013-9507-1
ISSN: 1874-2718
eISSN: 1874-270X
Version: Publisher Version
Status: Peer-reviewed
Type: Journal Article
Rights: Copyright © the authors, 2013. This article is distributed under the terms of the Creative Commons Attribution License which permits any use, distribution, and reproduction in any medium, provided the original author(s) and the source are credited.
Appears in Collections:Published Articles, Dept. of Biochemistry

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