A design for life: prokaryotic metal-binding MerR family regulators

Biometals. 2005 Aug;18(4):429-36. doi: 10.1007/s10534-005-3717-7.

Abstract

The MerR family of metal-binding, metal-responsive proteins is unique in that they activate transcription from unusual promoters and coordinate metals through cysteine (and in the case of ZntR, histidine) residues. They have conserved primary structures yet can effectively discriminate metals in vivo.

Publication types

  • Review

MeSH terms

  • Adenosine Triphosphatases / chemistry
  • Bacterial Proteins / chemistry
  • Bacterial Proteins / physiology*
  • Base Sequence
  • Crystallography, X-Ray
  • Cysteine / chemistry*
  • Cytoplasm / metabolism
  • DNA-Binding Proteins / chemistry
  • DNA-Binding Proteins / physiology*
  • Escherichia coli / metabolism*
  • Histidine / chemistry
  • Hydrogen Bonding
  • Metals / chemistry
  • Models, Biological
  • Models, Molecular
  • Molecular Sequence Data
  • Promoter Regions, Genetic
  • Sequence Homology, Nucleic Acid
  • Transcription Factors / chemistry
  • Transcription, Genetic

Substances

  • Bacterial Proteins
  • DNA-Binding Proteins
  • MerR protein, Bacteria
  • Metals
  • Transcription Factors
  • ZntR protein, bacteria
  • Histidine
  • Adenosine Triphosphatases
  • Cysteine