› 3sb2

X-ray diffraction
2.63Å resolution

Crystal Structure of the RNA chaperone Hfq from Herbaspirillum seropedicae SMR1

Released:
DOI: 10.2210/pdb3sb2/pdb
PDB entry 3sb2 coloured by chain, front view.
PDB entry 3sb2 coloured by chain, side view.
PDB entry 3sb2 coloured by chain, top view.
Source organism: Herbaspirillum seropedicae SmR1
Primary publication:
Structural characterization of the RNA chaperone Hfq from the nitrogen-fixing bacterium Herbaspirillum seropedicae SmR1.
Kadowaki MA, Iulek J, Barbosa JA, Pedrosa Fde O, de Souza EM, Chubatsu LS, Monteiro RA, de Oliveira MA, Steffens MB
Biochim Biophys Acta 1824 359-65 (2012)
PMID: 22154803

Function and Biology Details

Biochemical function:
Biological process:
Cellular component:
Sequence domains:

Structure analysis Details

Assembly composition:
homo hexamer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-112906 (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: 79 amino acids
Theoretical weight: 8.85 KDa
Source organism: Herbaspirillum seropedicae SmR1
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: D8IZU6 (Residues: 1-79; Coverage: 100%)
Gene names: Hsero_2948, hfq
Sequence domains: Hfq protein
Structure domains: SH3 type barrels.

Ligands and Environments

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

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU
Spacegroup: P21
Unit cell:
a: 59.639Å b: 65.323Å c: 60.987Å
α: 90° β: 105.47° γ: 90°
R-values:
R R work R free
0.203 0.199 0.28
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

2 review citations

The bacterial protein Hfq: much more than a mere RNA-binding factor.
Sobrero et al. (2012)
1 more

1 mention without citation

Haemophilus ducreyi Hfq contributes to virulence gene regulation as cells enter stationary phase.
Gangaiah et al. (2014)