› 3qo3

X-ray diffraction
2.15Å resolution

Crystal structure of Escherichia coli Hfq, in complex with ATP

Released:
DOI: 10.2210/pdb3qo3/pdb
PDB entry 3qo3 coloured by chain, front view.
PDB entry 3qo3 coloured by chain, side view.
PDB entry 3qo3 coloured by chain, top view.
Source organism: Escherichia coli K-12
Primary publication:
Structural and biochemical studies on ATP binding and hydrolysis by the Escherichia coli RNA chaperone Hfq.
Hämmerle H, Beich-Frandsen M, Večerek B, Rajkowitsch L, Carugo O, Djinović-Carugo K, Bläsi U
PLoS One 7 e50892 (2012)
PMID: 23226421

Function and Biology Details

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

Structure analysis Details

Assembly composition:
homo hexamer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-141440 (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: 65 amino acids
Theoretical weight: 7.33 KDa
Source organism: Escherichia coli K-12
Expression system: Escherichia coli
UniProt:
  • Canonical: P0A6X3 (Residues: 1-65; Coverage: 64%)
Gene names: JW4130, b4172, hfq
Sequence domains: Hfq protein
Structure domains: SH3 type barrels.

Ligands and Environments

1 bound ligand:
Ligand ATP 4 x ATP
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE ID14-1
Spacegroup: C2
Unit cell:
a: 104.3Å b: 40.62Å c: 100.81Å
α: 90° β: 101.81° γ: 90°
R-values:
R R work R free
0.229 0.228 0.257
Expression system: Escherichia coli

Quick links

Citations

6 review citations

Hfq chaperone brings speed dating to bacterial sRNA.
Santiago-Frangos et al. (2018)
5 more

2 mentions without citation

Structural analysis of full-length Hfq from Escherichia coli.
Beich-Frandsen et al. (2011)
1 more