期刊
SCIENCE
卷 301, 期 5638, 页码 1383-1387出版社
AMER ASSOC ADVANCEMENT SCIENCE
DOI: 10.1126/science.1085950
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资金
- NIDDK NIH HHS [F32 DK61868] Funding Source: Medline
- NIGMS NIH HHS [GM38784, R01 GM051350, GM51350, GM08382] Funding Source: Medline
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 +1 transition-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.
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