Structural highlights
Function
Q48428_KLEPN
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
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.
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 Also
References
- ↑ Shimizu-Ibuka A, Bauvois C, Sakai H, Galleni M. Structure of the plasmid-mediated class C beta-lactamase ACT-1. Acta Crystallogr Sect F Struct Biol Cryst Commun. 2008 May 1;64(Pt, 5):334-7. Epub 2008 Apr 5. PMID:18453698 doi:10.1107/S1744309108008531
