PDBe 4j6x

X-ray diffraction
2.22Å resolution

Crystal structure of Hfq from Pseudomonas aeruginosa in complex with UTP

Released:
Source organism: Pseudomonas aeruginosa PAO1
Primary publication:
Hfq binds ribonucleotides in three different RNA-binding sites.
Acta Crystallogr. D Biol. Crystallogr. 69 1504-13 (2013)
PMID: 23897473

Function and Biology Details

Biochemical function:
Biological process:
Cellular component:

Structure analysis Details

Assembly composition:
homo hexamer (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
RNA-binding protein Hfq Chains: A, B, C, D, E, F
Molecule details ›
Chains: A, B, C, D, E, F
Length: 82 amino acids
Theoretical weight: 9.11 KDa
Source organism: Pseudomonas aeruginosa PAO1
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: Q9HUM0 (Residues: 1-82; Coverage: 100%)
Gene names: PA4944, hfq
Sequence domains: Hfq protein
Structure domains: SH3 type barrels.

Ligands and Environments

1 bound ligand:

No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: BRUKER AXS MICROSTAR
Spacegroup: P212121
Unit cell:
a: 61.58Å b: 73.52Å c: 107.79Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.186 0.183 0.257
Expression system: Escherichia coli BL21(DE3)