Structure of the plasmid-mediated class C beta-lactamase ACT-1.
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.
Shimizu-Ibuka
Akiko
A
Department of Nutritional Science, Faculty of Applied Bio-Science, Tokyo University of Agriculture, Tokyo, Japan. a3shimizu@nodai.ac.jp
Bauvois
Cédric
C
Sakai
Hiroshi
H
Galleni
Moreno
M
D001426:Bacterial Proteins / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism; D001665:Binding Sites; D002876:Chromosomes, Bacterial / Q000235:genetics; D017931:DNA Primers; D016972:Enterobacter cloacae / Q000201:enzymology*; D004926:Escherichia coli / Q000201:enzymology*; D016297:Mutagenesis, Site-Directed; D010957:Plasmids / Q000235:genetics*; D011487:Protein Conformation; D001618:beta-Lactamases / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism
D001426:Bacterial Proteins; D017931:DNA Primers; C048795:AmpC beta-lactamases; D001618:beta-Lactamases; C494140:beta-lactamase MIR-1, Enterobacter cloacae