› 1exj

X-ray diffraction
3Å resolution

CRYSTAL STRUCTURE OF TRANSCRIPTION ACTIVATOR BMRR, FROM B. SUBTILIS, BOUND TO 21 BASE PAIR BMR OPERATOR AND TPP

Released:
DOI: 10.2210/pdb1exj/pdb
PDB entry 1exj coloured by chain, front view.
PDB entry 1exj coloured by chain, side view.
PDB entry 1exj coloured by chain, top view.
Source organism: Bacillus subtilis
Primary publication:
Crystal structure of the transcription activator BmrR bound to DNA and a drug.
Heldwein EE, Brennan RG
Nature 409 378-82 (2001)
PMID: 11201751

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-113777 (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: 278 amino acids
Theoretical weight: 32.62 KDa
Source organism: Bacillus subtilis
Expression system: Escherichia coli
UniProt:
  • Canonical: P39075 (Residues: 1-278; Coverage: 100%)
Gene names: BSU24020, bmr1R, bmrR
Sequence domains:
Structure domains:
DNA (5'-D(*AP*CP*CP*CP*TP*CP*CP*CP*CP*TP*TP*AP*GP*GP*GP*GP*AP*GP*GP*GP*T)-3') Chain: M
Molecule details ›
Chain: M
Length: 21 nucleotides
Theoretical weight: 6.44 KDa
Source organism: Bacillus subtilis
Expression system: Not provided

Ligands and Environments

3 bound ligands:
Ligand NA 1 x NA
Ligand ZN 1 x ZN
Ligand P4P 1 x P4P
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU RU300
Spacegroup: P4322
Unit cell:
a: 109.49Å b: 109.49Å c: 144.32Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.24 0.24 0.315
Expression systems:
  • Escherichia coli
  • Not provided

Quick links

Citations

47 review citations

The challenge of efflux-mediated antibiotic resistance in Gram-negative bacteria.
Li et al. (2015)
46 more

2 mentions without citation

Structural basis for gene regulation by a B12-dependent photoreceptor.
Jost et al. (2015)
1 more