2wiu

X-ray diffraction
2.35Å resolution

Mercury-modified bacterial persistence regulator hipBA

Released:
Source organism: Escherichia coli
Primary publication:
New kinase regulation mechanism found in HipBA: a bacterial persistence switch.
Acta Crystallogr. D Biol. Crystallogr. 65 875-9 (2009)
PMID: 19622872

Function and Biology Details

Structure analysis Details

Assembly composition:
hetero tetramer (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Serine/threonine-protein kinase toxin HipA Chains: A, C
Molecule details ›
Chains: A, C
Length: 446 amino acids
Theoretical weight: 50.17 KDa
Source organism: Escherichia coli
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: P23874 (Residues: 1-440; Coverage: 100%)
Gene names: JW1500, b1507, hipA
Sequence domains:
Antitoxin HipB Chains: B, D
Molecule details ›
Chains: B, D
Length: 88 amino acids
Theoretical weight: 10.02 KDa
Source organism: Escherichia coli
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: P23873 (Residues: 1-88; Coverage: 100%)
Gene names: JW1501, b1508, hipB
Sequence domains: Helix-turn-helix
Structure domains: lambda repressor-like DNA-binding domains

Ligands and Environments

2 bound ligands:

No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: NSLS BEAMLINE X25
Spacegroup: P4222
Unit cell:
a: 166.933Å b: 166.933Å c: 124.577Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.218 0.216 0.264
Expression system: Escherichia coli BL21(DE3)