High-resolution X-ray structure of an acyl-enzyme species for the class D OXA-10 beta-lactamase.
Beta-lactamases are resistance enzymes for beta-lactam antibiotics. These enzymes hydrolyze the beta-lactam moieties of these antibiotics, rendering them inactive. Of the four classes of known beta-lactamases, the enzymes of class D are the least understood. We report herein the high-resolution (1.9 A) crystal structure of the class D OXA-10 beta-lactamase inhibited by a penicillanate derivative. The structure provides evidence that the carboxylated Lys-70 (a carbamate) is intimately involved in the mechanism of the enzyme.
Maveyraud
Laurent
L
Groupe de Cristallographie Biologique, Institut de Pharmacologie et de Biologie Structurale du CNRS, 205 route de Narbonne, 31077-Toulouse Cedex, France.
Golemi-Kotra
Dasantila
D
Ishiwata
Akihiro
A
Meroueh
Oussama
O
Mobashery
Shahriar
S
Samama
Jean-Pierre
JP
D018360:Crystallography, X-Ray; D006863:Hydrogen-Ion Concentration; D007700:Kinetics; D008958:Models, Molecular; D019906:Nuclear Magnetic Resonance, Biomolecular; D011487:Protein Conformation; D065093:beta-Lactamase Inhibitors; D001618:beta-Lactamases / Q000737:chemistry* / Q000378:metabolism
D065093:beta-Lactamase Inhibitors; C425107:beta-lactamase OXA-10; D001618:beta-Lactamases