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

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 :

Issue :

Pt 5

Pages :

334-7

Peer reviewed :

Peer Reviewed verified by ORBi

Available on ORBi :

since 08 December 2015

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