3knr

Publication Abstract from PubMed

A number of multiresistant bacterial pathogens inactivate antibiotics by producing Zn(II)-dependent beta-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.

Metallo-beta-lactamases withstand low Zn(II) conditions by tuning metal-ligand interactions.,Gonzalez JM, Meini MR, Tomatis PE, Martin FJ, Cricco JA, Vila AJ Nat Chem Biol. 2012 Jun 24. doi: 10.1038/nchembio.1005. PMID:22729148^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.