1B4B
STRUCTURE OF THE OLIGOMERIZATION DOMAIN OF THE ARGININE REPRESSOR FROM BACILLUS STEAROTHERMOPHILUS
Summary for 1B4B
| Entry DOI | 10.2210/pdb1b4b/pdb |
| Descriptor | ARGININE REPRESSOR, ARGININE (3 entities in total) |
| Functional Keywords | repressor, arginine, core, oligomerization domain, helix turn helix |
| Biological source | Geobacillus stearothermophilus |
| Cellular location | Cytoplasm (Probable): O31408 |
| Total number of polymer chains | 3 |
| Total formula weight | 23448.45 |
| 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: 2024-10-23) |
| 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: 10331868DOI: 10.1038/8229 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.2 Å) |
Structure validation
Download full validation report
