› 1rq0

X-ray diffraction
2.65Å resolution

Crystal structure of peptide releasing factor 1

Released:
DOI: 10.2210/pdb1rq0/pdb
PDB entry 1rq0 coloured by chain, front view.
PDB entry 1rq0 coloured by chain, side view.
PDB entry 1rq0 coloured by chain, top view.
Source organism: Thermotoga maritima
Primary publication:
Structural analyses of peptide release factor 1 from Thermotoga maritima reveal domain flexibility required for its interaction with the ribosome.
Shin DH, Brandsen J, Jancarik J, Yokota H, Kim R, Kim SH
J Mol Biol 341 227-39 (2004)
PMID: 15312775

Function and Biology Details

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

Structure analysis Details

Assembly composition:
homo trimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-194772 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Peptide chain release factor 1 Chains: A, B, C
Molecule details ›
Chains: A, B, C
Length: 342 amino acids
Theoretical weight: 39.72 KDa
Source organism: Thermotoga maritima
Expression system: Escherichia coli
UniProt:
  • Canonical: Q9X183 (Residues: 1-342; Coverage: 100%)
Gene names: TM_1363, prfA
Sequence domains:
Structure domains:

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ALS BEAMLINE 5.0.2
Spacegroup: P21
Unit cell:
a: 51.9Å b: 137.23Å c: 80.93Å
α: 90° β: 106° γ: 90°
R-values:
R R work R free
0.224 0.216 0.294
Expression system: Escherichia coli

Quick links

Citations

17 review citations

Fidelity at the molecular level: lessons from protein synthesis.
Zaher et al. (2009)
16 more

6 mentions without citation

A functional peptidyl-tRNA hydrolase, ICT1, has been recruited into the human mitochondrial ribosome.
Richter et al. (2010)
5 more