› 4crm

Electron Microscopy
8.75Å resolution

Cryo-EM of a pre-recycling complex with eRF1 and ABCE1

Released:
DOI: 10.2210/pdb4crm/pdb
PDB entry 4crm coloured by chain, front view.
PDB entry 4crm coloured by chain, side view.
PDB entry 4crm coloured by chain, top view.
Source organism: Saccharomyces cerevisiae
Primary publication:
Cryoelectron microscopic structures of eukaryotic translation termination complexes containing eRF1-eRF3 or eRF1-ABCE1.
Preis A, Heuer A, Barrio-Garcia C, Hauser A, Eyler DE, Berninghausen O, Green R, Becker T, Beckmann R
Cell Rep 8 59-65 (2014)
PMID: 25001285
Related structures: EMD-2598

Function and Biology Details

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

Structure analysis Details

Assembly composition:
hetero dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-146159 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Translation initiation factor RLI1 Chain: P
Molecule details ›
Chain: P
Length: 608 amino acids
Theoretical weight: 68.43 KDa
Source organism: Saccharomyces cerevisiae
Expression system: Saccharomyces cerevisiae
UniProt:
  • Canonical: Q03195 (Residues: 1-608; Coverage: 100%)
Gene names: RLI1, YDR091C
Sequence domains:
Eukaryotic peptide chain release factor subunit 1 Chain: X
Molecule details ›
Chain: X
Length: 282 amino acids
Theoretical weight: 31.36 KDa
Source organism: Saccharomyces cerevisiae
Expression system: Escherichia coli
UniProt:
  • Canonical: P12385 (Residues: 140-421; Coverage: 65%)
Gene names: SAL4, SUP1, SUP45, YBR1120, YBR143C
Sequence domains:

Ligands and Environments

4 bound ligands:
Ligand ATP 1 x ATP
Ligand SF4 2 x SF4
Ligand ADP 1 x ADP
Ligand MG 1 x MG
No modified residues

Experiments and Validation Details

Entry percentile scores
Resolution: 8.75Å
Relevant EMDB volumes: EMD-2598
Expression systems:
  • Saccharomyces cerevisiae
  • Escherichia coli

Quick links

Citations

20 review citations

Nonsense-mediated mRNA decay: novel mechanistic insights and biological impact.
Karousis et al. (2016)
19 more

1 mention without citation

The ATPase mechanism of UvrA2 reveals the distinct roles of proximal and distal ATPase sites in nucleotide excision repair.
Case et al. (2019)