1B4A

STRUCTURE OF THE ARGININE REPRESSOR FROM BACILLUS STEAROTHERMOPHILUS

Summary for 1B4A

Entry DOI	10.2210/pdb1b4a/pdb
Descriptor	ARGININE REPRESSOR (2 entities in total)
Functional Keywords	repressor, arginine, helix turn helix
Biological source	Geobacillus stearothermophilus
Cellular location	Cytoplasm (Probable): O31408
Total number of polymer chains	6
Total formula weight	100857.27
Authors	Ni, J.,Sakanyan, V.,Charlier, D.,Glansdorff, N.,Van Duyne, G.D. (deposition date: 1998-12-18, release date: 1999-06-15, Last modification date: 2024-05-22)
Primary citation	Ni, J.,Sakanyan, V.,Charlier, D.,Glansdorff, N.,Van Duyne, G.D. Structure of the arginine repressor from Bacillus stearothermophilus. Nat.Struct.Biol., 6:427-432, 1999 Cited by PubMed Abstract: 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. PubMed: 10331868 DOI: 10.1038/8229 PDB entries with the same primary citation
Experimental method	X-RAY DIFFRACTION (2.5 Å)

Structure validation