Solution structure of the DNA-binding domain and model for the complex of multifunctiona hexameric arginine represser with DNA

• DOI: 10.1038/nsb1097-819
• Publication Date: 2004-08-19T15:39:58Z
• Authors: Maria Sunnerhagen; Michael Nilges; Gottfried Otting; Jannette Carey
• Keywords: Models, Molecular; 0303 health sciences; Binding Sites; Base Sequence; Macromolecular Substances; Escherichia coli Proteins; Molecular Sequence Data; DNA; Protein Structure, Secondary; Recombinant Proteins; DNA-Binding Proteins; Repressor Proteins; Solutions; 03 medical and health sciences; Bacterial Proteins; Nucleic Acid Conformation; Amino Acid Sequence; Cloning, Molecular; Nuclear Magnetic Resonance, Biomolecular; Helix-Turn-Helix Motifs

The structure of the monomeric DNA-binding domain of the Escherichia coli arginine repressor, ArgR, determined by NMR spectroscopy, shows structural homology to the winged helix-turn-helix (wHTH) family, a motif found in a diverse class of proteins including both gene regulators and gene organizers from prokaryotes and eukaryotes. Biochemical data on DNA binding by intact ArgR are used as constraints to position the domain on its DNA target and to derive a model for the hexamer-DNA complex using the known structure of the L-arginine-binding domain. The structural independence of the wHTH fold may be important for multimeric DNA-binding proteins that contact extended DNA regions with imperfect match to consensus sequences, a feature of many wHTH-domain proteins.