› 3iao

X-ray diffraction
2.8Å resolution

Conformational plasticity of the coiled coil domain of BmrR is required for bmr promoter binding-the unliganded structure of BmrR

Released:
DOI: 10.2210/pdb3iao/pdb
PDB entry 3iao coloured by chain, front view.
PDB entry 3iao coloured by chain, side view.
PDB entry 3iao coloured by chain, top view.
Source organism: Bacillus subtilis
Primary publication:
Conformational plasticity of the coiled-coil domain of BmrR is required for bmr operator binding: the structure of unliganded BmrR.
Kumaraswami M, Newberry KJ, Brennan RG
J Mol Biol 398 264-75 (2010)
PMID: 20230832

Function and Biology Details

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

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: 278 amino acids
Theoretical weight: 32.59 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:

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ALS BEAMLINE 8.3.1
Spacegroup: I4122
Unit cell:
a: 168Å b: 168Å c: 63.1Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.241 0.241 0.275
Expression system: Escherichia coli

Quick links

Citations

1 review citation

Bacterial gold sensing and resistance.
Checa et al. (2011)
12 other articles

6 mentions without citation

Diversity of Cyclic Di-GMP-Binding Proteins and Mechanisms.
Chou et al. (2016)
5 more