Structural highlights
Function
[ARGR_GEOSE] Regulates arginine biosynthesis genes.
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 arginine repressor (ArgR) is a hexameric DNA-binding protein that plays a multifunctional role in the bacterial cell. Here, we present the 2.5 A structure of apo-ArgR from Bacillus stearothermophilus and the 2.2 A structure of the hexameric ArgR oligomerization domain with bound arginine. This first view of intact ArgR reveals an approximately 32-symmetric hexamer of identical subunits, with six DNA-binding domains surrounding a central oligomeric core. The difference in quaternary organization of subunits in the arginine-bound and apo forms provides a possible explanation for poor operator binding by apo-ArgR and for high affinity binding in the presence of arginine.
Structure of the arginine repressor from Bacillus stearothermophilus.,Ni J, Sakanyan V, Charlier D, Glansdorff N, Van Duyne GD Nat Struct Biol. 1999 May;6(5):427-32. PMID:10331868[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Ni J, Sakanyan V, Charlier D, Glansdorff N, Van Duyne GD. Structure of the arginine repressor from Bacillus stearothermophilus. Nat Struct Biol. 1999 May;6(5):427-32. PMID:10331868 doi:http://dx.doi.org/10.1038/8229
