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

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.

SUBMITTER: Shimizu-Ibuka A

PROVIDER: S-EPMC2376412 | biostudies-literature | 2008 May

REPOSITORIES: biostudies-literature

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

Shimizu-Ibuka Akiko A Bauvois Cédric C Sakai Hiroshi H Galleni Moreno M

Acta crystallographica. Section F, Structural biology and crystallization communications 20080405 Pt 5

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. ...[more]

PMID: 18453698

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