› 1gqe

X-ray diffraction
1.81Å resolution

Polypeptide Chain Release Factor 2 (RF2) from Escherichia coli

Released:
DOI: 10.2210/pdb1gqe/pdb
PDB entry 1gqe coloured by chain, front view.
PDB entry 1gqe coloured by chain, side view.
PDB entry 1gqe coloured by chain, top view.
Source organism: Escherichia coli K-12
Primary publication:
Bacterial polypeptide release factor RF2 is structurally distinct from eukaryotic eRF1.
Vestergaard B, Van LB, Andersen GR, Nyborg J, Buckingham RH, Kjeldgaard M
Mol Cell 8 1375-82 (2001)
PMID: 11779511

Function and Biology Details

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

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-139336 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Peptide chain release factor RF2 Chain: A
Molecule details ›
Chain: A
Length: 365 amino acids
Theoretical weight: 41.68 KDa
Source organism: Escherichia coli K-12
Expression system: Escherichia coli
UniProt:
  • Canonical: P07012 (Residues: 1-365; Coverage: 100%)
Gene names: JW5847, b2891, prfB, supK
Sequence domains:
Structure domains:

Ligands and Environments

No bound ligands
1 modified residue:
Ligand MSE 9 x MSE

Experiments and Validation Details

Entry percentile scores
X-ray source: ELETTRA BEAMLINE 5.2R
Spacegroup: P21
Unit cell:
a: 57.388Å b: 49.893Å c: 63.144Å
α: 90° β: 107.01° γ: 90°
R-values:
R R work R free
0.222 0.222 0.247
Expression system: Escherichia coli

Quick links

Citations

27 review citations

Ribosome structure and the mechanism of translation.
Ramakrishnan V. (2002)
26 more

16 mentions without citation

Dynamic basis of fidelity and speed in translation: Coordinated multistep mechanisms of elongation and termination.
Prabhakar et al. (2017)
15 more