› 1qde

X-ray diffraction
2Å resolution

CRYSTAL STRUCTURE OF THE ATPASE DOMAIN OF TRANSLATION INITIATION FACTOR 4A FROM SACCHAROMYCES CEREVISIAE-THE PROTOTYPE OF THE DEAD BOX PROTEIN FAMILY

Released:
DOI: 10.2210/pdb1qde/pdb
PDB entry 1qde coloured by chain, front view.
PDB entry 1qde coloured by chain, side view.
PDB entry 1qde coloured by chain, top view.
Source organism: Saccharomyces cerevisiae
Primary publication:
Crystal structure of the ATPase domain of translation initiation factor 4A from Saccharomyces cerevisiae--the prototype of the DEAD box protein family.
Benz J, Trachsel H, Baumann U
Structure 7 671-9 (1999)
PMID: 10404596

Function and Biology Details

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

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-145154 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
ATP-dependent RNA helicase eIF4A Chain: A
Molecule details ›
Chain: A
Length: 224 amino acids
Theoretical weight: 25.17 KDa
Source organism: Saccharomyces cerevisiae
Expression system: Escherichia coli
UniProt:
  • Canonical: P10081 (Residues: 9-232; Coverage: 57%)
Gene names: J0660, TIF1, TIF2, TIF41A, TIF41B, YJL138C, YKR059W
Sequence domains: DEAD/DEAH box helicase
Structure domains: P-loop containing nucleotide triphosphate hydrolases

Ligands and Environments

1 bound ligand:
Ligand SO4 1 x SO4
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU RU200
Spacegroup: P212121
Unit cell:
a: 38.88Å b: 59.28Å c: 92.05Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.214 0.214 0.266
Expression system: Escherichia coli

Quick links

Citations

15 review citations

The DEAD-box protein family of RNA helicases.
Cordin et al. (2006)
14 more

7 mentions without citation

Crystal structure of the yeast eIF4A-eIF4G complex: an RNA-helicase controlled by protein-protein interactions.
Schütz et al. (2008)
6 more