2bg2
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BACILLUS CEREUS METALLO-BETA-LACTAMASE (BCII) ARG (121) CYS MUTANT. SOLVED AT PH4.5 USING 20MM ZNSO4 IN THE BUFFER. 1MM DTT AND 1MM TCEP-HCL WERE USED AS REDUCING AGENTS. CYS221 IS REDUCED.
OverviewOverview
The zinc-dependent metallo-beta-lactamases are a group of bacterial, enzymes that pose a threat to the future efficacy of present-day, antibiotics. Their mechanism is poorly understood, and there are no, clinically useful inhibitors. While most members of the group contain two, tightly bound zinc ions in their active sites, the Bacillus cereus enzyme, has a much lower affinity for its second zinc (Zn2), thought to be due to, the presence of Arg121 immediately beneath the floor of the active site, (cf. Cys/Ser/His121 in the bizinc enzymes). Crystal structures of the, Arg121Cys mutant of the B. cereus 569/H/9 enzyme were solved at pH 7.0, 5.0, and 4.5, each in the presence of either 20 microM or 20 mM Zn(2+) to, generate the mono- and bizinc forms, respectively. Surprisingly, the, structure ... [(full description)]
About this StructureAbout this Structure
2BG2 is a [Single protein] structure of sequence from [Bacillus cereus] with ZN, SO4, CL and GOL as [ligands]. Active as [Beta-lactamase], with EC number [3.5.2.6]. Structure known Active Site: AC1. Full crystallographic information is available from [OCA].
ReferenceReference
Effect of pH on the active site of an Arg121Cys mutant of the metallo-beta-lactamase from Bacillus cereus: implications for the enzyme mechanism., Davies AM, Rasia RM, Vila AJ, Sutton BJ, Fabiane SM, Biochemistry. 2005 Mar 29;44(12):4841-9. PMID:15779910
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