Issue 5, 2010

Coordinating intracellularnickel–metal-site structure-function relationships and the NikR and RcnR repressors

Abstract

Covering: up to the end of 2009

Metalloregulator function requires both sensitivity and selectivity to ensure metal-specific activity without interfering with intracellular metal trafficking pathways. Here, we examine the role of metal-coordination geometry in the function of NikR and RcnR, two widely conserved nickel-responsive regulators that are both present in E. coli. The available data suggest an emerging trend in which coordination number is linked to metal-binding affinity, and thus regulatory function. The differences in coordination geometry also suggest that the kinetic mechanisms of metal-association and dissociation will contribute to metalloregulator function. We also discuss ways in which the ligand-binding properties of metalloregulators may be tuned to alter the regulatory response.

Graphical abstract: Coordinating intracellular nickel–metal-site structure-function relationships and the NikR and RcnR repressors

Article information

Article type
Review Article
Submitted
09 Dec 2009
First published
05 Mar 2010

Nat. Prod. Rep., 2010,27, 658-667

Coordinating intracellular nickel–metal-site structure-function relationships and the NikR and RcnR repressors

J. S. Iwig and P. T. Chivers, Nat. Prod. Rep., 2010, 27, 658 DOI: 10.1039/B906683G

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