PMID:12958362
| Citation |
Changela, A, Chen, K, Xue, Y, Holschen, J, Outten, CE, O'Halloran, TV and Mondragón, A (2003) Molecular basis of metal-ion selectivity and zeptomolar sensitivity by CueR. Science 301:1383-7 |
|---|---|
| Abstract |
The earliest of a series of copper efflux genes in Escherichia coli are controlled by CueR, a member of the MerR family of transcriptional activators. Thermodynamic calibration of CueR reveals a zeptomolar (10(-21) molar) sensitivity to free Cu+, which is far less than one atom per cell. Atomic details of this extraordinary sensitivity and selectivity for +1transition-metal ions are revealed by comparing the crystal structures of CueR and a Zn2+-sensing homolog, ZntR. An unusual buried metal-receptor site in CueR restricts the metal to a linear, two-coordinate geometry and uses helix-dipole and hydrogen-bonding interactions to enhance metal binding. This binding mode is rare among metalloproteins but well suited for an ultrasensitive genetic switch. |
| Links |
PubMed Online version:10.1126/science.1085950 |
| Keywords |
Amino Acid Sequence; Bacterial Proteins/chemistry; Bacterial Proteins/genetics; Bacterial Proteins/metabolism; Binding Sites; Copper/metabolism; Crystallization; Crystallography, X-Ray; DNA-Binding Proteins/chemistry; DNA-Binding Proteins/genetics; DNA-Binding Proteins/metabolism; Dimerization; Escherichia coli/chemistry; Escherichia coli/genetics; Escherichia coli/metabolism; Escherichia coli Proteins/chemistry; Escherichia coli Proteins/genetics; Escherichia coli Proteins/metabolism; Helix-Turn-Helix Motifs; Hydrogen Bonding; Hydrophobic and Hydrophilic Interactions; Ligands; Metals/metabolism; Models, Molecular; Molecular Sequence Data; Oxidation-Reduction; Promoter Regions, Genetic; Protein Conformation; Protein Structure, Secondary; Sequence Alignment; Thermodynamics; Transcription Factors/chemistry; Transcription Factors/genetics; Transcription Factors/metabolism; Transcriptional Activation; Zinc/metabolism |
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