Article
The MerR metalloregulatory protein binds mercuric ion as a tricoordinate, metal-bridged dimer.
Science (New York, N.Y.) - 23 Feb 1990
Helmann J D, Ballard B T, Walsh C T
Abstract excerpt
Bacterial MerR proteins are dimeric DNA-binding proteins that mediate the Hg(II)-dependent induction of mercury resistance operons. Site-directed mutagenesis of the Bacillus sp. RC607 MerR protein reveals that three of four Cys residues per monomer are required for Hg(II) binding at the single high-affinity binding site. Inactive mutant homodimers can exchange subunits to form heterodimers active for Hg(II)...
Topics
- Amino Acid Sequence
- Bacillus
- Bacterial Proteins
- Base Sequence
- Binding Sites
- Cations
- DNA-Binding Proteins
- Macromolecular Substances
- Mercury
- Molecular Sequence Data
- Mutation