› 4kbf

X-ray diffraction
1.9Å resolution

two different open conformations of the helicase core of the RNA helicase Hera

Released:
DOI: 10.2210/pdb4kbf/pdb
PDB 4kbf coloured by chain and viewed from the front.
PDB 4kbf coloured by chain and viewed from the side.
PDB 4kbf coloured by chain and viewed from the top.
Source organism: Thermus thermophilus HB27
Primary publication:
Rearranging RNA structures at 75°C? towards the molecular mechanism and physiological function of the Thermus thermophilus DEAD-box helicase hera.
Klostermeier D
Biopolymers (2013)
PMID: 23765433

Function and Biology Details

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

Structure analysis Details

Assemblies composition:
monomeric
homo dimer (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Heat resistant RNA dependent ATPase Chains: A, B
Molecule details ›
Chains: A, B
Length: 365 amino acids
Theoretical weight: 40 KDa
Source organism: Thermus thermophilus HB27
Expression system: Escherichia coli
UniProt:
  • Canonical: Q72GF3 (Residues: 8-372; Coverage: 71%)
Gene name: TT_C1895
Sequence domains:
Structure domains: P-loop containing nucleotide triphosphate hydrolases

Ligands and Environments

3 bound ligands:
Ligand AMP 1 x AMP
Ligand NA 2 x NA
Ligand SO4 1 x SO4
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SLS BEAMLINE X10SA
Spacegroup: P43212
Unit cell:
a: 119.645Å b: 119.645Å c: 107.095Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.192 0.19 0.218
Expression system: Escherichia coli

Quick links

Citations

1 review citation

RNA helicase proteins as chaperones and remodelers.
Jarmoskaite et al. (2014)
3 other articles