1dxk
From Proteopedia
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METALLO-BETA-LACTAMASE FROM BACILLUS CEREUS 569/H/9 C168S MUTANT
Overview
Beta-lactamases are involved in bacterial resistance. Members of the, metallo-enzyme class are now found in many pathogenic bacteria and are, becoming thus of major clinical importance. Despite the availability of, Zn-beta-lactamase X-ray structures their mechanism of action is still, unclear. One puzzling observation is the presence of one or two zincs in, the active site. To aid in assessing the role of zinc content in, beta-lactam hydrolysis, the replacement by Ser of the zinc-liganding, residue Cys168 in the Zn-beta-lactamase from Bacillus cereus strain, 569/H/9 was carried out: the mutant enzyme (C168S) is inactive in the, mono-Zn form, but active in the di-Zn form. The structure of the mono-Zn, form of the C168S mutant has been determined at 1.85 A resolution. Ser168, occupies the ... [(full description)]
About this Structure
1DXK is a [Single protein] structure of sequence from [Bacillus cereus] with ZN and BCT as [ligands]. Active as [[1]], with EC number [3.5.2.6]. Full crystallographic information is available from [OCA].
Reference
Structural effects of the active site mutation cysteine to serine in Bacillus cereus zinc-beta-lactamase., Chantalat L, Duee E, Galleni M, Frere JM, Dideberg O, Protein Sci. 2000 Jul;9(7):1402-6. PMID:10933508
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