2ylb

X-ray diffraction
1.15Å resolution

Structure of Salmonella typhimurium Hfq at 1.15 A

Released:
Primary publication:
Structural basis for RNA 3'-end recognition by Hfq.
Proc. Natl. Acad. Sci. U.S.A. 108 13065-70 (2011)
PMID: 21737752

Function and Biology Details

Biochemical function:
Cellular component:
  • not assigned

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: 74 amino acids
Theoretical weight: 8.26 KDa
Source organism: Salmonella enterica subsp. enterica serovar Typhimurium str. LT2
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: P0A1R0 (Residues: 1-72; Coverage: 71%)
Gene names: STM4361, hfq
Sequence domains: Hfq protein
Structure domains: SH3 type barrels.

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SLS BEAMLINE X10SA
Spacegroup: P61
Unit cell:
a: 61.4Å b: 61.4Å c: 167.03Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.17 0.168 0.208
Expression system: Escherichia coli BL21(DE3)