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CRYSTAL STRUCTURE OF THE CLASS D BETA-LACTAMASE OXA-10

Overview

We report the crystal structure of a class D beta-lactamase, the broad, spectrum enzyme OXA-10 from Pseudomonas aeruginosa at 2.0 A resolution., There are significant differences between the overall fold observed in, this structure and those of the evolutionarily related class A and class C, beta-lactamases. Furthermore, the structure suggests the unique, cation, mediated formation of a homodimer. Kinetic and hydrodynamic data shows, that the dimer is a relevant species in solution and is the more active, form of the enzyme. Comparison of the molecular details of the active, sites of the class A and class C enzymes with the OXA-10 structure reveals, that there is no counterpart in OXA-10 to the residues proposed to act as, general bases in either of these enzymes (Glu 166 and Tyr 150, respectively). Our structures of the native and chloride inhibited forms, of OXA-10 suggest that the class D enzymes have evolved a distinct, catalytic mechanism for beta-lactam hydrolysis. Clinical variants of, OXA-10 are also discussed in light of the structure.

About this Structure

1FOF is a Single protein structure of sequence from Pseudomonas aeruginosa with CO and SO4 as ligands. Active as Beta-lactamase, with EC number 3.5.2.6 Full crystallographic information is available from OCA.

Reference

Crystal structure of the class D beta-lactamase OXA-10., Paetzel M, Danel F, de Castro L, Mosimann SC, Page MG, Strynadka NC, Nat Struct Biol. 2000 Oct;7(10):918-25. PMID:11017203

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