The MerR metalloregulatory protein binds mercuric ion as a tricoordinate, metal-bridged dimer.
Science
; 247(4945): 946-8, 1990 Feb 23.
Article
em En
| MEDLINE
| ID: mdl-2305262
ABSTRACT
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) binding. Studies of a heterodimer retaining only three of eight cysteine residues per dimer reveal that Cys79 in one subunit and Cys114 and Cys123 in the second subunit are necessary and sufficient for high-affinity Hg(II) binding in an asymmetric, subunit bridging coordination complex.
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Base de dados:
MEDLINE
Assunto principal:
Bacillus
/
Proteínas de Bactérias
/
Proteínas de Ligação a DNA
/
Mercúrio
Idioma:
En
Ano de publicação:
1990
Tipo de documento:
Article