Bacterial Proteins/chemistry/genetics/metabolism; Binding Sites; Chromosomes, Bacterial/genetics; DNA Primers; Enterobacter cloacae/enzymology; Escherichia coli/enzymology; Mutagenesis, Site-Directed; Plasmids/genetics; Protein Conformation; beta-Lactamases/chemistry/genetics/metabolism
Abstract :
[en] The crystallographic structure of ACT-1, which is the first plasmid-mediated AmpC-type beta-lactamase to have been completely analyzed in terms of nucleotide sequence and which has a high degree of sequence similarity to the chromosomal AmpC enzymes of Enterobacter cloacae and the plasmid-encoded MIR-1, has been solved at 2.4 A resolution. The overall structure of ACT-1 is similar to those of other class C beta-lactamases, such as the AmpC enzymes from E. cloacae P99 and Escherichia coli.
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