A design for life: prokaryotic metal-binding MerR family regulators.
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.
Hobman
Jon L
JL
School of Biosciences, The University of Birmingham, Edgbaston, UK. J.L.Hobman@bham.ac.uk
Wilkie
John
J
Brown
Nigel L
NL
D000251:Adenosine Triphosphatases / Q000737:chemistry; D001426:Bacterial Proteins / Q000737:chemistry / Q000502:physiology*; D001483:Base Sequence; D018360:Crystallography, X-Ray; D003545:Cysteine / Q000737:chemistry*; D003593:Cytoplasm / Q000378:metabolism; D004268:DNA-Binding Proteins / Q000737:chemistry / Q000502:physiology*; D004926:Escherichia coli / Q000378:metabolism*; D006639:Histidine / Q000737:chemistry; D006860:Hydrogen Bonding; D008670:Metals / Q000737:chemistry; D008954:Models, Biological; D008958:Models, Molecular; D008969:Molecular Sequence Data; D011401:Promoter Regions, Genetic; D012689:Sequence Homology, Nucleic Acid; D014157:Transcription Factors / Q000737:chemistry; D014158:Transcription, Genetic
D001426:Bacterial Proteins; D004268:DNA-Binding Proteins; C051124:MerR protein, Bacteria; D008670:Metals; D014157:Transcription Factors; C118628:ZntR protein, bacteria; D006639:Histidine; D000251:Adenosine Triphosphatases; D003545:Cysteine