› 3d6y

X-ray diffraction
2.7Å resolution

Crystal structure of R275E mutant of BMRR bound to DNA and berberine

Released:
DOI: 10.2210/pdb3d6y/pdb
PDB entry 3d6y coloured by chain, front view.
PDB entry 3d6y coloured by chain, side view.
PDB entry 3d6y coloured by chain, top view.
Source organisms:
Primary publication:
Structures of BmrR-drug complexes reveal a rigid multidrug binding pocket and transcription activation through tyrosine expulsion.
Newberry KJ, Huffman JL, Miller MC, Vazquez-Laslop N, Neyfakh AA, Brennan RG
J Biol Chem 283 26795-804 (2008)
PMID: 18658145

Function and Biology Details

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

Structure analysis Details

Assembly composition:
hetero tetramer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-116171 (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: 33.45 KDa
Source organism: Bacillus subtilis
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: P39075 (Residues: 1-278; Coverage: 100%)
Gene names: BSU24020, bmr1R, bmrR
Sequence domains:
Structure domains:
BMR promoter DNA Chain: B
Molecule details ›
Chain: B
Length: 24 nucleotides
Theoretical weight: 7.36 KDa
Source organism: synthetic construct
Expression system: Not provided

Ligands and Environments

2 bound ligands:
Ligand BER 1 x BER
Ligand GOL 2 x GOL
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ALS BEAMLINE 8.2.1
Spacegroup: P4322
Unit cell:
a: 106.33Å b: 106.33Å c: 146.75Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.227 0.227 0.259
Expression systems:
  • Escherichia coli BL21(DE3)
  • Not provided

Quick links

Citations

4 review citations

Coordination chemistry of bacterial metal transport and sensing.
Ma et al. (2009)
3 more

4 mentions without citation

The Recognition of Identical Ligands by Unrelated Proteins.
Barelier et al. (2015)
3 more