1AOY
N-TERMINAL DOMAIN OF ESCHERICHIA COLI ARGININE REPRESSOR NMR, 23 STRUCTURES
Summary for 1AOY
| Entry DOI | 10.2210/pdb1aoy/pdb |
| Descriptor | ARGININE REPRESSOR (1 entity in total) |
| Functional Keywords | dna-binding protein, expression regulation, dna organization, winged helix, dna binding protein |
| Biological source | Escherichia coli |
| Total number of polymer chains | 1 |
| Total formula weight | 8722.12 |
| Authors | Sunnerhagen, M.,Nilges, M.,Otting, G. (deposition date: 1997-07-14, release date: 1997-09-17, Last modification date: 2024-04-10) |
| Primary citation | Sunnerhagen, M.,Nilges, M.,Otting, G.,Carey, J. Solution structure of the DNA-binding domain and model for the complex of multifunctional hexameric arginine repressor with DNA. Nat.Struct.Biol., 4:819-826, 1997 Cited by PubMed Abstract: 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. PubMed: 9334747DOI: 10.1038/nsb1097-819 PDB entries with the same primary citation |
| Experimental method | SOLUTION NMR |
Structure validation
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