1pio
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(New page: 200px<br /><applet load="1pio" size="450" color="white" frame="true" align="right" spinBox="true" caption="1pio, resolution 2.8Å" /> '''AN ENGINEERED STAPHYL...)
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Revision as of 21:43, 20 November 2007
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AN ENGINEERED STAPHYLOCOCCUS AUREUS PC1 BETA-LACTAMASE THAT HYDROLYSES THIRD GENERATION CEPHALOSPORINS
Overview
The beta-lactamase from Staphylococcus aureus PC1 has been cloned into an, Escherichia coli vector for site-directed mutagenesis and high-level, protein expression. A mutant enzyme has been produced in which Ala238 is, replaced by a serine, and Ile239 is deleted (A238S:I239del). The, engineered enzyme hydrolyses third-generation cephalosporins substantially, more rapidly than the parental enzyme does, while hydrolysis of, benzylpenicillin is slower with the mutant than with the wild-type and, native enzymes. The mutant beta-lactamase has been crystallized and the, structure determined and refined at 2.8 A resolution. The disposition of, the beta-strand which forms the side of the active site is altered in, comparison with the native S. aureus beta-lactamase structure, widening, the active site cleft and providing space to accommodate the bulky, side-chains of the third-generation cephalosporins.
About this Structure
1PIO is a Single protein structure of sequence from Staphylococcus aureus. Active as Beta-lactamase, with EC number 3.5.2.6 Full crystallographic information is available from OCA.
Reference
An engineered Staphylococcus aureus PC1 beta-lactamase that hydrolyses third-generation cephalosporins., Zawadzke LE, Smith TJ, Herzberg O, Protein Eng. 1995 Dec;8(12):1275-85. PMID:8869640
Page seeded by OCA on Tue Nov 20 23:50:39 2007
