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

Nat Prod Rep. 2010 May;27(5):658-67. doi: 10.1039/b906683g. Epub 2010 Mar 5.

Abstract

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.

Publication types

  • Research Support, U.S. Gov't, Non-P.H.S.
  • Review

MeSH terms

  • Bacterial Proteins / metabolism*
  • Escherichia coli Proteins / metabolism*
  • Models, Biological
  • Nickel* / chemistry
  • Nickel* / metabolism
  • Repressor Proteins / metabolism*
  • Structure-Activity Relationship

Substances

  • Bacterial Proteins
  • Escherichia coli Proteins
  • NikR protein, E coli
  • Repressor Proteins
  • ferric uptake regulating proteins, bacterial
  • Nickel