› 1f9n

X-ray diffraction
2.7Å resolution

CRYSTAL STRUCTURE OF AHRC, THE ARGININE REPRESSOR/ACTIVATOR PROTEIN FROM BACILLUS SUBTILIS

Released:
DOI: 10.2210/pdb1f9n/pdb
PDB entry 1f9n coloured by chain, front view.
PDB entry 1f9n coloured by chain, side view.
PDB entry 1f9n coloured by chain, top view.
Source organism: Bacillus subtilis
Primary publication:
The structure of AhrC, the arginine repressor/activator protein from Bacillus subtilis.
Dennis C CA, Glykos NM, Parsons MR, Phillips SE
Acta Crystallogr D Biol Crystallogr 58 421-30 (2002)
PMID: 11856827

Function and Biology Details

Biochemical function:
Biological process:
Cellular component:
Sequence domains:
Structure domains:

Structure analysis Details

Assembly composition:
homo hexamer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-148205 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Arginine repressor Chains: A, B, C, D, E, F
Molecule details ›
Chains: A, B, C, D, E, F
Length: 149 amino acids
Theoretical weight: 16.85 KDa
Source organism: Bacillus subtilis
Expression system: Escherichia coli
UniProt:
  • Canonical: P17893 (Residues: 1-149; Coverage: 100%)
Gene names: BSU24250, ahrC, argR
Sequence domains:
Structure domains:

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SRS BEAMLINE PX9.6
Spacegroup: C2221
Unit cell:
a: 230.31Å b: 73.86Å c: 138.9Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.22 0.22 0.27
Expression system: Escherichia coli

Quick links

Citations

1 review citation

Pathways and regulation of bacterial arginine metabolism and perspectives for obtaining arginine overproducing strains.
Lu et al. (2006)
14 other articles

8 mentions without citation

Listeria monocytogenes 10403S Arginine Repressor ArgR Finely Tunes Arginine Metabolism Regulation under Acidic Conditions.
Cheng et al. (2017)
7 more