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Crystal Structure of Class C beta-Lactamase ACT-1Crystal Structure of Class C beta-Lactamase ACT-1
Structural highlights
FunctionEvolutionary Conservation![]() Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedThe 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. Structure of the plasmid-mediated class C beta-lactamase ACT-1.,Shimizu-Ibuka A, Bauvois C, Sakai H, Galleni M Acta Crystallogr Sect F Struct Biol Cryst Commun. 2008 May 1;64(Pt, 5):334-7. Epub 2008 Apr 5. PMID:18453698[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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