› 4i67

X-ray diffraction
2.33Å resolution

Crystal structure of the RRM domain of RNA helicase HERA from T. thermophilus in complex with GGGC RNA

Released:
DOI: 10.2210/pdb4i67/pdb
PDB entry 4i67 coloured by chain, front view.
PDB entry 4i67 coloured by chain, side view.
PDB entry 4i67 coloured by chain, top view.
Source organism: Thermus thermophilus
Primary publication:
Recognition of two distinct elements in the RNA substrate by the RNA-binding domain of the T. thermophilus DEAD box helicase Hera.
Steimer L, Wurm JP, Linden MH, Rudolph MG, Wöhnert J, Klostermeier D
Nucleic Acids Res 41 6259-72 (2013)
PMID: 23625962

Function and Biology Details

Reaction catalysed: 
ATP + H(2)O = ADP + phosphate
Biochemical function:
  • not assigned
Biological process:
  • not assigned
Cellular component:
  • not assigned

Structure analysis Details

Assembly composition:
hetero dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-180805 (preferred)
Entry contents:
1 distinct polypeptide molecule
1 distinct RNA molecule
Macromolecules (2 distinct):
Heat resistant RNA dependent ATPase Chain: A
Molecule details ›
Chain: A
Length: 87 amino acids
Theoretical weight: 9.58 KDa
Source organism: Thermus thermophilus
Expression system: Escherichia coli
UniProt:
  • Canonical: Q72GF3 (Residues: 431-517; Coverage: 17%)
Gene name: TT_C1895
Structure domains: Alpha-Beta Plaits
5'-R(P*GP*GP*GP*(RPC))-3' Chain: B
Molecule details ›
Chain: B
Length: 4 nucleotides
Theoretical weight: 1.38 KDa
Source organism: Thermus thermophilus
Expression system: Not provided

Ligands and Environments

No bound ligands
1 modified residue:
Ligand RPC 1 x RPC

Experiments and Validation Details

Entry percentile scores
X-ray source: SLS BEAMLINE X10SA
Spacegroup: P61
Unit cell:
a: 88.435Å b: 88.435Å c: 28.943Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.179 0.177 0.234
Expression systems:
  • Escherichia coli
  • Not provided

Quick links

Citations

3 review citations

RNA helicase proteins as chaperones and remodelers.
Jarmoskaite et al. (2014)
2 more

3 mentions without citation

Evidence for cooperative tandem binding of hnRNP C RRMs in mRNA processing.
Cieniková et al. (2015)
2 more