› 3tb6

X-ray diffraction
2.21Å resolution

Structure of the effector-binding domain of arabinose repressor AraR from Bacillus subtilis

Released:
DOI: 10.2210/pdb3tb6/pdb
PDB entry 3tb6 coloured by chain, front view.
PDB entry 3tb6 coloured by chain, side view.
PDB entry 3tb6 coloured by chain, top view.
Source organism: Bacillus subtilis
Primary publication:
Structure of the effector-binding domain of the arabinose repressor AraR from Bacillus subtilis.
Procházková K, Cermáková K, Pachl P, Sieglová I, Fábry M, Otwinowski Z, Rezáčová P
Acta Crystallogr D Biol Crystallogr 68 176-85 (2012)
PMID: 22281747

Function and Biology Details

Biochemical function:
  • not assigned
Biological process:
Cellular component:
  • not assigned
Sequence domains:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-161244 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Arabinose metabolism transcriptional repressor Chains: A, B
Molecule details ›
Chains: A, B
Length: 298 amino acids
Theoretical weight: 33.39 KDa
Source organism: Bacillus subtilis
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: P96711 (Residues: 71-362; Coverage: 81%)
Gene names: BSU33970, araC, araR, yvbS
Sequence domains: Periplasmic binding protein-like domain
Structure domains: Rossmann fold

Ligands and Environments

2 bound ligands:
Ligand ARB 2 x ARB
Ligand GOL 2 x GOL
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: BESSY BEAMLINE 14.2
Spacegroup: P212121
Unit cell:
a: 62.068Å b: 106.333Å c: 111.847Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.188 0.186 0.231
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

1 review citation

Allosteric control of transcription in GntR family of transcription regulators: A structural overview.
Jain D. (2015)
7 other articles

1 mention without citation

Structure of the effector-binding domain of the arabinose repressor AraR from Bacillus subtilis.
Procházková et al. (2012)