› 4w7s

X-ray diffraction
2.54Å resolution

Crystal structure of the yeast DEAD-box splicing factor Prp28 at 2.54 Angstroms resolution

Released:
DOI: 10.2210/pdb4w7s/pdb
PDB entry 4w7s coloured by chain, front view.
PDB entry 4w7s coloured by chain, side view.
PDB entry 4w7s coloured by chain, top view.
Source organism: Saccharomyces cerevisiae S288C
Primary publication:
Crystal structure, mutational analysis and RNA-dependent ATPase activity of the yeast DEAD-box pre-mRNA splicing factor Prp28.
Jacewicz A, Schwer B, Smith P, Shuman S
Nucleic Acids Res 42 12885-98 (2014)
PMID: 25303995

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 analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-149950 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Pre-mRNA-splicing ATP-dependent RNA helicase PRP28 Chains: A, B
Molecule details ›
Chains: A, B
Length: 463 amino acids
Theoretical weight: 52.99 KDa
Source organism: Saccharomyces cerevisiae S288C
Expression system: Escherichia coli
UniProt:
  • Canonical: P23394 (Residues: 127-588; Coverage: 79%)
Gene names: PRP28, YD8419.10C, YDR243C
Sequence domains:
Structure domains: P-loop containing nucleotide triphosphate hydrolases

Ligands and Environments

4 bound ligands:
Ligand P6G 8 x P6G
Ligand GOL 1 x GOL
Ligand ANP 1 x ANP
Ligand MG 2 x MG
1 modified residue:
Ligand MSE 24 x MSE

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 24-ID-C
Spacegroup: P3221
Unit cell:
a: 114.719Å b: 114.719Å c: 156.186Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.169 0.166 0.219
Expression system: Escherichia coli

Quick links

Citations

2 review citations

The organization and contribution of helicases to RNA splicing.
De et al. (2016)
1 more

5 mentions without citation

Prespliceosome structure provides insights into spliceosome assembly and regulation.
Plaschka et al. (2018)
4 more