› 2e29

Solution NMR

Solution structure of the GUCT domain from human ATP-dependent RNA helicase DDX50, DEAD box protein 50

Released:
DOI: 10.2210/pdb2e29/pdb
PDB entry 2e29 coloured by chain, ensemble of 20 models, front view.
PDB entry 2e29 coloured by chain, ensemble of 20 models, side view.
PDB entry 2e29 coloured by chain, ensemble of 20 models, top view.
Source organism: Homo sapiens
Primary publication:
Solution structure of the GUCT domain from human RNA helicase II/Gu beta reveals the RRM fold, but implausible RNA interactions.
Ohnishi S, Pääkkönen K, Koshiba S, Tochio N, Sato M, Kobayashi N, Harada T, Watanabe S, Muto Y, Güntert P, Tanaka A, Kigawa T, Yokoyama S
Proteins 74 133-44 (2009)
PMID: 18615715

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-189661 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
ATP-dependent RNA helicase DDX50 Chain: A
Molecule details ›
Chain: A
Length: 92 amino acids
Theoretical weight: 10.15 KDa
Source organism: Homo sapiens
Expression system: Cell-free protein synthesis
UniProt:
  • Canonical: Q9BQ39 (Residues: 575-659; Coverage: 12%)
Gene name: DDX50
Sequence domains: GUCT (NUC152) domain
Structure domains: Alpha-Beta Plaits

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
Refinement method: torsion angle dynamics, restrained molecular dynamics
Expression system: Cell-free protein synthesis

Quick links

Citations

1 review citation

The mechanism of ATP-dependent RNA unwinding by DEAD box proteins.
Hilbert et al. (2009)
7 other articles

3 mentions without citation

Host DDX Helicases as Possible SARS-CoV-2 Proviral Factors: A Structural Overview of Their Hijacking Through Multiple Viral Proteins.
Squeglia et al. (2020)
2 more