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

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.