1PIO

AN ENGINEERED STAPHYLOCOCCUS AUREUS PC1 BETA-LACTAMASE THAT HYDROLYSES THIRD GENERATION CEPHALOSPORINS

Summary for 1PIO

• Entry DOI: 10.2210/pdb1pio/pdb
• Descriptor: BETA-LACTAMASE (2 entities in total)
• Functional Keywords: hydrolase (acting on cyclic amides)
• Biological source: Staphylococcus aureus
• Total number of polymer chains: 2
• Total formula weight: 57754.50

Authors

Zawadzke, L.E.,Herzberg, O. (deposition date: 1995-10-11, release date: 1996-03-08, Last modification date: 2024-05-22)

Primary citation

Zawadzke, L.E.,Smith, T.J.,Herzberg, O.
An engineered Staphylococcus aureus PC1 beta-lactamase that hydrolyses third-generation cephalosporins.
Protein Eng., 8:1275-1285, 1995

PubMed Abstract: 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.

PubMed: 8869640
DOI: 10.1093/protein/8.12.1275

Experimental method

X-RAY DIFFRACTION (2.8 Å)