1. Metallo-?-lactamases withstand low Zn(II) conditions by tuning metal-ligand interactions.
- Author
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González, Javier M, Meini, María-Rocío, Tomatis, Pablo E, Martín, Francisco J Medrano, Cricco, Julia A, and Vila, Alejandro J
- Subjects
BETA lactamases ,ZINC ,METAL ions ,ANTIBIOTICS ,CHEMICAL kinetics ,ENZYME activation ,CHEMICAL affinity ,LIGAND binding (Biochemistry) - Abstract
A number of multiresistant bacterial pathogens inactivate antibiotics by producing Zn(II)-dependent ?-lactamases. We show that metal uptake leading to an active dinuclear enzyme in the periplasmic space of Gram-negative bacteria is ensured by a cysteine residue, an unusual metal ligand in oxidizing environments. Kinetic, structural and affinity data show that such Zn(II)-cysteine interaction is an adaptive trait that tunes the metal binding affinity, thus enabling antibiotic resistance at restrictive Zn(II) concentrations. [ABSTRACT FROM AUTHOR]
- Published
- 2012
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