Structure of the plasmid-mediated class C beta-lactamase ACT-1

Acta Crystallogr Sect F Struct Biol Cryst Commun. 2008 May 1;64(Pt 5):334-7. doi: 10.1107/S1744309108008531. Epub 2008 Apr 5.

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.

Publication types

  • Comparative Study

MeSH terms

  • Bacterial Proteins / chemistry*
  • Bacterial Proteins / genetics
  • Bacterial Proteins / metabolism
  • Binding Sites
  • Chromosomes, Bacterial / genetics
  • DNA Primers
  • Enterobacter cloacae / enzymology*
  • Escherichia coli / enzymology*
  • Mutagenesis, Site-Directed
  • Plasmids / genetics*
  • Protein Conformation
  • beta-Lactamases / chemistry*
  • beta-Lactamases / genetics
  • beta-Lactamases / metabolism

Substances

  • Bacterial Proteins
  • DNA Primers
  • AmpC beta-lactamases
  • beta-Lactamases
  • beta-lactamase MIR-1, Enterobacter cloacae