X-ray diffraction
3.1Å resolution

Crystal structure of BmrR bound to Acetylcholine

Source organism: Bacillus subtilis
Primary publication:
Structural contributions to multidrug recognition in the multidrug resistance (MDR) gene regulator, BmrR.
Proc. Natl. Acad. Sci. U.S.A. 108 11046-51 (2011)
PMID: 21690368

Function and Biology Details

Structure analysis Details

Assembly composition:
hetero tetramer (preferred)
Entry contents:
1 distinct polypeptide molecule
1 distinct DNA molecule
Macromolecules (2 distinct):
Multidrug-efflux transporter 1 regulator Chain: A
Molecule details ›
Chain: A
Length: 284 amino acids
Theoretical weight: 33.48 KDa
Source organism: Bacillus subtilis
Expression system: Escherichia coli
  • Canonical: P39075 (Residues: 1-278; Coverage: 100%)
Gene names: BSU24020, bmr1R, bmrR
Sequence domains:
Structure domains:
23 bp promoter DNA Chain: B
Molecule details ›
Chain: B
Length: 23 nucleotides
Theoretical weight: 7.06 KDa
Source organism: Bacillus subtilis
Expression system: Not provided

Ligands and Environments

2 bound ligands:

No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SSRL BEAMLINE BL9-2
Spacegroup: P4322
Unit cell:
a: 106.407Å b: 106.407Å c: 145.571Å
α: 90° β: 90° γ: 90°
R R work R free
0.227 0.225 0.276
Expression systems:
  • Escherichia coli
  • Not provided