IBR   13079
INSTITUTO DE BIOLOGIA MOLECULAR Y CELULAR DE ROSARIO
Unidad Ejecutora - UE
congresos y reuniones científicas
Título:
THE METALLO-BETA-LACTAMASE GOB IS A MONO-Zn(II) ENZYME WITH A NOVEL ACTIVE SITE
Autor/es:
MARÍA NATALIA LISA, JORGELINA MORÁN BARRIO, JAVIER M. GONZALEZ, ALISON L.COSTELLO, DAVID L. TIERNEY, ADRIANA S. LIMANSKY, ALEJANDRO M. VIALE AND ALEJANDRO J. VILA
Lugar:
Montevideo-Uruguay
Reunión:
Congreso; 6th International Conference of Biological Physics ICBP 2007, 5th Southern Cone Biophysics Congress and 34th Annual Meeting of the Argentinean Biophysical Society; 2007
Institución organizadora:
Sociedad Argentina de Biofisica
Resumen:
Metallo-β-lactamases (MβLs) are zinc dependent enzymes able to hydrolyze and inactivatemost β-lactam antibiotics. The large diversity of active site structures and metal contentamong MβLs from different sources has limited the design of a pan-MβL inhibitor. Herewe report the biochemical and biophysical characterization of a novel MβL, GOB-18, froma clinical isolate of a Gram-negative opportunistic pathogen, Elizabethkingiameningoseptica. Spectroscopic data obtained on the native and metal substituted enzyme,and mutagenesis experiments, reveal that the metal ion is bound to Asp120, His121,His263, and a solvent molecule, i.e., in the canonical Zn2 site of dinuclear MβLs.Contrasting all other related MβLs, GOB-18 is fully active against a broad range of β-lactam substrates using a single Zn(II) ion in this site. These data further enlarge thestructural diversity of MβLs.