Abstract
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.
MeSH terms
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Bacterial Proteins / chemistry*
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Bacterial Proteins / genetics
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Bacterial Proteins / metabolism
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Binding Sites
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Chromosomes, Bacterial / genetics
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DNA Primers
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Enterobacter cloacae / enzymology*
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Escherichia coli / enzymology*
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Mutagenesis, Site-Directed
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Plasmids / genetics*
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Protein Conformation
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beta-Lactamases / chemistry*
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beta-Lactamases / genetics
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beta-Lactamases / metabolism
Substances
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Bacterial Proteins
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DNA Primers
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AmpC beta-lactamases
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beta-Lactamases
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beta-lactamase MIR-1, Enterobacter cloacae