Coordinating intracellular nickel-metal-site structure-function relationships and the NikR and RcnR repressors.
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.
Iwig
Jeffrey S
JS
Department of Biochemistry and Molecular Biophysics, Washington University School of Medicine, St. Louis, USA.
Chivers
Peter T
PT
D001426:Bacterial Proteins / Q000378:metabolism*; D029968:Escherichia coli Proteins / Q000378:metabolism*; D008954:Models, Biological; D009532:Nickel / Q000737:chemistry / Q000378:metabolism; D012097:Repressor Proteins / Q000378:metabolism*; D013329:Structure-Activity Relationship
D001426:Bacterial Proteins; D029968:Escherichia coli Proteins; C402409:NikR protein, E coli; D012097:Repressor Proteins; C068477:ferric uptake regulating proteins, bacterial; D009532:Nickel