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 prokaryotypes 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.
|Original language||English (US)|
|Number of pages||8|
|Journal||Nature Structural Biology|
|State||Published - Oct 22 1997|
All Science Journal Classification (ASJC) codes
- Structural Biology