期刊
NATURE CHEMICAL BIOLOGY
卷 8, 期 8, 页码 698-700出版社
NATURE PUBLISHING GROUP
DOI: 10.1038/NCHEMBIO.1005
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资金
- CONICET
- Howard Hughes Medical Institute
- Agencia Nacional de Promocion Cientifica y Tecnologica
- US National Institutes of Health [1R01AI100560]
- Laboratorio Nacional de Luz Sincrotron, Campinas, Brazil
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.
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