Article (Scientific journals)
Complete 1H, 15N and 13C resonance assignments of Bacillus cereus metallo-b-lactamase and its complex with the inhibitor R-thiomandelic acid
Karsisiotis, Andreas Ioannis; Damblon, Christian; Roberts, Gordon C K
2014In Biomolecular NMR Assignments, 8, p. 313-318
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Keywords :
Metallo-b-lactamase; R-thiomandelic acid; BcII; BcII–inhibitor complex
Abstract :
[en] b-Lactamases inactivate b-lactam antibiotics by hydrolysis of their endocyclic b-lactam bond and are a major cause of antibiotic resistance in pathogenic bacteria. The zinc dependent metallo-b-lactamase enzymes are of particular concern since they are located on highly transmissible plasmids and have a broad spectrum of activity against almost all b-lactam antibiotics. We present here essentially complete ([96 %) backbone and sidechain sequence-specific NMR resonance assignments for the Bacillus cereus subclass B1 metallo-b-lactamase, BcII, and for its complex with R-thiomandelic acid, a broad spectrum inhibitor of metallo-b-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-b-lactamase inhibitors.
Disciplines :
Chemistry
Author, co-author :
Karsisiotis, Andreas Ioannis
Damblon, Christian ;  Université de Liège - ULiège > Département de chimie (sciences) > Chimie biologique structurale
Roberts, Gordon C K
Language :
English
Title :
Complete 1H, 15N and 13C resonance assignments of Bacillus cereus metallo-b-lactamase and its complex with the inhibitor R-thiomandelic acid
Publication date :
2014
Journal title :
Biomolecular NMR Assignments
ISSN :
1874-2718
eISSN :
1874-270X
Publisher :
Springer, Dordrecht, Netherlands
Volume :
8
Pages :
313-318
Peer reviewed :
Peer Reviewed verified by ORBi
Available on ORBi :
since 18 December 2014

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