1b4b

STRUCTURE OF THE OLIGOMERIZATION DOMAIN OF THE ARGININE REPRESSOR FROM BACILLUS STEAROTHERMOPHILUS

spinqualitylabelsall models 1b4b, resolution 2.20Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 1b4b is a 3 chain structure with sequence from Geobacillus stearothermophilus. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 2.2Å Ligands: ARG Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT 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 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Arginine repressor 3D structures

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