› 5ae5

X-ray diffraction
2.64Å resolution

Structures of inactive and activated DntR provide conclusive evidence for the mechanism of action of LysR transcription factors

Released:
DOI: 10.2210/pdb5ae5/pdb
PDB entry 5ae5 coloured by chain, front view.
PDB entry 5ae5 coloured by chain, side view.
PDB entry 5ae5 coloured by chain, top view.
Source organism: Burkholderia cepacia
Primary publication:
The solution configurations of inactive and activated DntR have implications for the sliding dimer mechanism of LysR transcription factors.
Lerche M, Dian C, Round A, Lönneborg R, Brzezinski P, Leonard GA
OpenAccess logo Sci Rep 6 19988 (2016)
PMID: 26817994

Function and Biology Details

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

Structure analysis Details

Assembly composition:
homo tetramer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-566270 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
HTH lysR-type domain-containing protein Chains: A, B
Molecule details ›
Chains: A, B
Length: 308 amino acids
Theoretical weight: 34.87 KDa
Source organism: Burkholderia cepacia
Expression system: Escherichia coli M15
UniProt:
  • Canonical: Q7WT50 (Residues: 1-301; Coverage: 100%)
Gene name: dntR
Sequence domains:

Ligands and Environments

1 bound ligand:
Ligand GOL 9 x GOL
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE ID29
Spacegroup: P6522
Unit cell:
a: 107.132Å b: 107.132Å c: 297.844Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.201 0.199 0.227
Expression system: Escherichia coli M15

Quick links

Citations

2 review citations

Metallochaperones and metalloregulation in bacteria.
Capdevila et al. (2017)
1 more

4 mentions without citation

Cell-Wall Recycling of the Gram-Negative Bacteria and the Nexus to Antibiotic Resistance.
Dik et al. (2018)
3 more