› 2vgm

X-ray diffraction
2.6Å resolution

Structure of S. cerevisiae Dom34, a translation termination-like factor involved in RNA quality control pathways and interacting with Hbs1 (Unlabeled protein)

Released:
DOI: 10.2210/pdb2vgm/pdb
PDB entry 2vgm coloured by chain, front view.
PDB entry 2vgm coloured by chain, side view.
PDB entry 2vgm coloured by chain, top view.
Source organism: Saccharomyces cerevisiae S288C
Primary publication:
Structure of yeast Dom34: a protein related to translation termination factor Erf1 and involved in No-Go decay.
Graille M, Chaillet M, van Tilbeurgh H
J Biol Chem 283 7145-54 (2008)
PMID: 18180287

Function and Biology Details

Biochemical function:
Biological process:
Cellular component:
Sequence domains:
Structure domains:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-152581 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Protein DOM34 Chain: A
Molecule details ›
Chain: A
Length: 386 amino acids
Theoretical weight: 44.12 KDa
Source organism: Saccharomyces cerevisiae S288C
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: P33309 (Residues: 1-386; Coverage: 100%)
Gene names: DOM34, N2016, YNL001W
Sequence domains:
Structure domains:

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE BM30A
Spacegroup: P3221
Unit cell:
a: 75.5Å b: 75.5Å c: 163.981Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.226 0.226 0.288
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

19 review citations

RNA degradation in Saccharomyces cerevisae.
Parker R. (2012)
18 more

3 mentions without citation

Recent structural studies on Dom34/aPelota and Hbs1/aEF1α: important factors for solving general problems of ribosomal stall in translation.
Kobayashi et al. (2013)
2 more