1aoy
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| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
N-TERMINAL DOMAIN OF ESCHERICHIA COLI ARGININE REPRESSOR NMR, 23 STRUCTURES
OverviewOverview
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.
About this StructureAbout this Structure
1AOY is a Single protein structure of sequence from Escherichia coli. Full crystallographic information is available from OCA.
ReferenceReference
Solution structure of the DNA-binding domain and model for the complex of multifunctional hexameric arginine repressor with DNA., Sunnerhagen M, Nilges M, Otting G, Carey J, Nat Struct Biol. 1997 Oct;4(10):819-26. PMID:9334747
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