2ZC7

Crystal Structure of Class C beta-Lactamase ACT-1

Summary for 2ZC7

• Entry DOI: 10.2210/pdb2zc7/pdb
• Descriptor: Beta-lactamase ACT-1 (2 entities in total)
• Functional Keywords: two-domain structure, hydrolase
• Biological source: Klebsiella pneumoniae
• Total number of polymer chains: 4
• Total formula weight: 157287.81

Authors

Shimizu-Ibuka, A.,Sakai, H.,Galleni, M. (deposition date: 2007-11-02, release date: 2008-09-23, Last modification date: 2023-11-01)

Primary citation

Shimizu-Ibuka, A.,Bauvois, C.,Sakai, H.,Galleni, M.
Structure of the plasmid-mediated class C beta-lactamase ACT-1
Acta Crystallogr.,Sect.F, 64:334-337, 2008

PubMed 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.

PubMed: 18453698
DOI: 10.1107/S1744309108008531

Experimental method

X-RAY DIFFRACTION (2.4 Å)