› 3p27

X-ray diffraction
2.95Å resolution

Crystal structure of S. cerevisiae Hbs1 protein (GDP-bound form), a translational GTPase involved in RNA quality control pathways and interacting with Dom34/Pelota

Released:
DOI: 10.2210/pdb3p27/pdb
PDB entry 3p27 coloured by chain, front view.
PDB entry 3p27 coloured by chain, side view.
PDB entry 3p27 coloured by chain, top view.
Source organism: Saccharomyces cerevisiae
Primary publication:
Dissection of Dom34-Hbs1 reveals independent functions in two RNA quality control pathways.
van den Elzen AM, Henri J, Lazar N, Gas ME, Durand D, Lacroute F, Nicaise M, van Tilbeurgh H, Séraphin B, Graille M
Nat Struct Mol Biol 17 1446-52 (2010)
PMID: 21102444

Function and Biology Details

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

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-152443 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Elongation factor 1 alpha-like protein Chains: A, B
Molecule details ›
Chains: A, B
Length: 483 amino acids
Theoretical weight: 54.84 KDa
Source organism: Saccharomyces cerevisiae
Expression system: Escherichia coli
UniProt:
  • Canonical: P32769 (Residues: 135-611; Coverage: 78%)
Gene names: HBS1, YKR084C, YKR404
Sequence domains: Elongation factor Tu GTP binding domain
Structure domains:

Ligands and Environments

1 bound ligand:
Ligand GDP 2 x GDP
1 modified residue:
Ligand MSE 20 x MSE

Experiments and Validation Details

Entry percentile scores
X-ray source: SOLEIL BEAMLINE PROXIMA 1
Spacegroup: P42212
Unit cell:
a: 109.964Å b: 109.964Å c: 188.199Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.217 0.214 0.278
Expression system: Escherichia coli

Quick links

Citations

13 review citations

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

1 mention without citation

Structural insights into ribosomal rescue by Dom34 and Hbs1 at near-atomic resolution.
Hilal et al. (2016)