2bg8

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spinqualitylabelsall models 2bg8, resolution 2.5Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image

BACILLUS CEREUS METALLO-BETA-LACTAMASE (BCII) ARG (121) CYS MUTANT. SOLVED AT PH4.5 USING 20 MICROMOLAR ZNSO4 IN THE BUFFER. 1MM DTT AND 1MM TCEP-HCL WERE USED AS REDUCING AGENTS.

Overview

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 Structure

2BG8 is a [Protein complex] structure of sequences from [Bacillus cereus] with ZN, SO4 and GOL as [ligands]. Active as [[1]], with EC number [3.5.2.6]. Full crystallographic information is available from [OCA].

Reference

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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