1gce
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STRUCTURE OF THE BETA-LACTAMASE OF ENTEROBACTER CLOACAE GC1
OverviewOverview
A class C beta-lactamase from a clinical isolate of Enterobacter cloacae, strain GC1 with improved hydrolytic activity for oxyimino beta-lactam, antibiotics has been analyzed by X-ray crystallography to 1.8 A, resolution. Relative to the wild-type P99 beta-lactamase, this natural, mutant contains a highly unique tandem repeat Ala211-Val212-Arg213 [Nugaka, et al. (1995) J. Biol. Chem. 270, 5729-5735]. The 39.4 kDa chromosomal, beta-lactamase crystallizes from poly(ethylene glycol) 8000 in potassium, phosphate in space group P2(1)2(1)2 with cell dimensions a = 78.0 A, b =, 69.5 A, and c = 63.1 A. The crystal structure was solved by the molecular, replacement method, and the model has been refined to an R-factor of 0.20, for all nonzero data from 8 to 1.8 A. Deviations of model bonds and ... [(full description)]
About this StructureAbout this Structure
1GCE is a [Single protein] structure of sequence from [Enterobacter cloacae]. Active as [[1]], with EC number [3.5.2.6]. Full crystallographic information is available from [OCA].
ReferenceReference
Structure of the extended-spectrum class C beta-lactamase of Enterobacter cloacae GC1, a natural mutant with a tandem tripeptide insertion., Crichlow GV, Kuzin AP, Nukaga M, Mayama K, Sawai T, Knox JR, Biochemistry. 1999 Aug 10;38(32):10256-61. PMID:10441119
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