Complete ^sup 1^H, ^sup 15^N and ^sup 13^C resonance assignments of Bacillus cereus metallo-[beta]-lactamase and its complex with the inhibitor R-thiomandelic acid

[beta]-Lactamases inactivate [beta]-lactam antibiotics by hydrolysis of their endocyclic [beta]-lactam bond and are a major cause of antibiotic resistance in pathogenic bacteria. The zinc dependent metallo-[beta]-lactamase enzymes are of particular concern since they are located on highly transmissi...

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Bibliographic Details
Published in:Biomolecular NMR assignments 2014-10, Vol.8 (2), p.313
Main Authors: Karsisiotis, Andreas Ioannis, Damblon, Christian, Roberts, Gordon C, K
Format: Article
Language:English
Subjects:
Bacteria
Drug resistance
Enzymes
NMR
Nuclear magnetic resonance
Online Access:Get full text
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Summary:[beta]-Lactamases inactivate [beta]-lactam antibiotics by hydrolysis of their endocyclic [beta]-lactam bond and are a major cause of antibiotic resistance in pathogenic bacteria. The zinc dependent metallo-[beta]-lactamase enzymes are of particular concern since they are located on highly transmissible plasmids and have a broad spectrum of activity against almost all [beta]-lactam antibiotics. We present here essentially complete (>96 %) backbone and sidechain sequence-specific NMR resonance assignments for the Bacillus cereus subclass B1 metallo-[beta]-lactamase, BcII, and for its complex with R-thiomandelic acid, a broad spectrum inhibitor of metallo-[beta]-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-[beta]-lactamase inhibitors.[PUBLICATION ABSTRACT]
ISSN:1874-2718
1874-270X
DOI:10.1007/s12104-013-9507-1