1ome: Difference between revisions
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Revision as of 16:53, 30 October 2007
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CRYSTAL STRUCTURE OF THE OMEGA LOOP DELETION MUTANT (RESIDUES 163-178 DELETED) OF BETA-LACTAMASE FROM STAPHYLOCOCCUS AUREUS PC1
OverviewOverview
The structure of class A beta-lactamases contains an omega-loop associated, with the active site, which carries a key catalytic residue, Glu166. A, 16-residue omega-loop deletion mutant of beta-lactamase from, Staphylococcus aureus PC1, encompassing residues 163-178, was produced in, order to examine the functional and structural role of the loop. The, crystal structure was determined and refined at 2.3 A, and the kinetics of, the mutant enzyme was characterized with a variety of beta-lactam, antibiotics. In general, the wild-type beta-lactamase hydrolyzes, penicillin compounds better than cephalosporins. In contrast, the deletion, of the omega-loop led to a variant enzyme that acts only on, cephalosporins, including third generation compounds. Kinetic measurements, and electrospray mass ... [(full description)]
About this StructureAbout this Structure
1OME is a [Single protein] structure of sequence from [Staphylococcus aureus] with CL as [ligand]. Active as [Beta-lactamase], with EC number [3.5.2.6]. Structure known Active Site: CAT. Full crystallographic information is available from [OCA].
ReferenceReference
Role of the omega-loop in the activity, substrate specificity, and structure of class A beta-lactamase., Banerjee S, Pieper U, Kapadia G, Pannell LK, Herzberg O, Biochemistry. 1998 Mar 10;37(10):3286-96. PMID:9521648
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