Structural highlights
Function
[ARGR_ECOLI] Negatively controls the expression of the four operons of arginine biosynthesis in addition to the carAB operon. Predominantly interacts with A/T residues in ARG boxes. It also binds to a specific site in cer locus. Thus it is essential for cer-mediated site-specific recombination in ColE1. It is necessary for monomerization of the plasmid ColE1.
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
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.
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[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ 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. 1997 Oct;4(10):819-26. PMID:9334747
