Article (Scientific journals)
Structure of the plasmid-mediated class C beta-lactamase ACT-1.
Shimizu-Ibuka, Akiko; Bauvois, Cedric; Sakai, Hiroshi et al.
2008In Acta Crystallographica. Section F, Structural Biology and Crystallization Communications, 64 (Pt 5), p. 334-7
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Keywords :
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.
Disciplines :
Biochemistry, biophysics & molecular biology
Author, co-author :
Shimizu-Ibuka, Akiko
Bauvois, Cedric
Sakai, Hiroshi
Galleni, Moreno ;  Université de Liège - ULiège
Language :
English
Title :
Structure of the plasmid-mediated class C beta-lactamase ACT-1.
Publication date :
2008
Journal title :
Acta Crystallographica. Section F, Structural Biology and Crystallization Communications
eISSN :
1744-3091
Publisher :
International Union of Crystallography, United Kingdom
Volume :
64
Issue :
Pt 5
Pages :
334-7
Peer reviewed :
Peer Reviewed verified by ORBi
Available on ORBi :
since 08 December 2015

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