› 2fx0

X-ray diffraction
2.4Å resolution

Crystal Structure of HlyIIR, a Hemolysin II transcriptional Regulator

Released:
DOI: 10.2210/pdb2fx0/pdb
PDB entry 2fx0 coloured by chain, front view.
PDB entry 2fx0 coloured by chain, side view.
PDB entry 2fx0 coloured by chain, top view.
Source organism: Bacillus cereus
Primary publication:
Crystal structure of Bacillus cereus HlyIIR, a transcriptional regulator of the gene for pore-forming toxin hemolysin II.
Kovalevskiy OV, Lebedev AA, Surin AK, Solonin AS, Antson AA
J Mol Biol 365 825-34 (2007)
PMID: 17097673

Function and Biology Details

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

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-182182 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
HTH tetR-type domain-containing protein Chain: A
Molecule details ›
Chain: A
Length: 201 amino acids
Theoretical weight: 23.58 KDa
Source organism: Bacillus cereus
Expression system: Escherichia coli
UniProt:
  • Canonical: Q7X506 (Residues: 1-201; Coverage: 100%)
Gene names: CQZ91_02635, hlyIIR
Sequence domains:
Structure domains:

Ligands and Environments

No bound ligands
1 modified residue:
Ligand MSE 4 x MSE

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE BM14
Spacegroup: P6122
Unit cell:
a: 124.208Å b: 124.208Å c: 79.667Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.223 0.221 0.276
Expression system: Escherichia coli

Quick links

Citations

1 review citation

The pore-forming haemolysins of bacillus cereus: a review.
Ramarao et al. (2013)
6 other articles

4 mentions without citation

Glucose 6P binds and activates HlyIIR to repress Bacillus cereus haemolysin hlyII gene expression.
Guillemet et al. (2013)
3 more