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Crystal structure of KorA bound to operator DNA: insight into repressor cooperation in RP4 gene regulation
- Source :
- Nucleic Acids Research
- Publication Year :
- 2009
-
Abstract
- KorA is a global repressor in RP4 which regulates cooperatively the expression of plasmid genes whose products are involved in replication, conjugative transfer and stable inheritance. The structure of KorA bound to an 18-bp DNA duplex that contains the symmetric operator sequence and incorporates 5-bromo-deoxyuridine nucleosides has been determined by multiple-wavelength anomalous diffraction phasing at 1.96-Å resolution. KorA is present as a symmetric dimer and contacts DNA via a helix–turn–helix motif. Each half-site of the symmetric operator DNA binds one copy of the protein in the major groove. As confirmed by mutagenesis, recognition specificity is based on two KorA side chains forming hydrogen bonds to four bases within each operator half-site. KorA has a unique dimerization module shared by the RP4 proteins TrbA and KlcB. We propose that these proteins cooperate with the global RP4 repressor KorB in a similar manner via this dimerization module and thus regulate RP4 inheritance.
- Subjects :
- DNA, Bacterial
Models, Molecular
Cancer Research
Operator Regions, Genetic
Stereochemistry
Molecular Sequence Data
Repressor
Biology
Crystallography, X-Ray
DNA-binding protein
chemistry.chemical_compound
Plasmid
Bacterial Proteins
Structural Biology
Genetics
Amino Acid Sequence
Binding site
Peptide sequence
Gene
Regulation of gene expression
Binding Sites
Gene Expression Regulation, Bacterial
Protein Structure, Tertiary
DNA-Binding Proteins
Repressor Proteins
chemistry
Nucleic Acid Conformation
Protein Multimerization
DNA
Plasmids
Subjects
Details
- Language :
- English
- Database :
- OpenAIRE
- Journal :
- Nucleic Acids Research
- Accession number :
- edsair.doi.dedup.....e153eec209fd7683f546f4c608cccd91