1B4A: Structure Of The Arginine Repressor From Bacillus Stearothermophilus

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.
PDB ID: 1B4ADownload
MMDB ID: 10442
PDB Deposition Date: 1998/12/18
Updated in MMDB: 2011/11
Experimental Method:
x-ray diffraction
Resolution: 2.5  Å
Source Organism:
Similar Structures:
Biological Unit for 1B4A: hexameric; determined by author and by software (PISA)
Molecular Components in 1B4A
Label Count Molecule
Proteins (6 molecules)
Arginine Repressor
Molecule annotation
* Click molecule labels to explore molecular sequence information.

Citing MMDB