› 1bow

X-ray diffraction
2.7Å resolution

MULTIDRUG-BINDING DOMAIN OF TRANSCRIPTION ACTIVATOR BMRR (APO FORM)

Released:
DOI: 10.2210/pdb1bow/pdb
PDB entry 1bow coloured by chain, front view.
PDB entry 1bow coloured by chain, side view.
PDB entry 1bow coloured by chain, top view.
Source organism: Bacillus subtilis
Primary publication:
Structural basis of multidrug recognition by BmrR, a transcription activator of a multidrug transporter.
Zheleznova EE, Markham PN, Neyfakh AA, Brennan RG
Cell 96 353-62 (1999)
PMID: 10025401

Function and Biology Details

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

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-153820 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Multidrug-efflux transporter 1 regulator Chain: A
Molecule details ›
Chain: A
Length: 159 amino acids
Theoretical weight: 18.49 KDa
Source organism: Bacillus subtilis
Expression system: Escherichia coli
UniProt:
  • Canonical: P39075 (Residues: 121-278; Coverage: 57%)
Gene names: BSU24020, bmr1R, bmrR
Sequence domains: GyrI-like small molecule binding domain
Structure domains: Regulatory factor, effector binding domain

Ligands and Environments

1 bound ligand:
Ligand MN 1 x MN
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU RUH2R
Spacegroup: P41212
Unit cell:
a: 76.3Å b: 76.3Å c: 96Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.202 not available 0.27
Expression system: Escherichia coli

Quick links

Citations

36 review citations

Multiple molecular mechanisms for multidrug resistance transporters.
Higgins CF. (2007)
35 more

1 mention without citation

Structures of BmrR-drug complexes reveal a rigid multidrug binding pocket and transcription activation through tyrosine expulsion.
Newberry et al. (2008)