1oms

X-ray diffraction
2.3Å resolution

Structure determination by MAD: E.coli Trigger Factor binding at the ribosomal exit tunnel.

Released:
Source organism: Escherichia coli
Primary publication:
Chaperone binding at the ribosomal exit tunnel.
Structure 11 1547-56 (2003)
PMID: 14656439

Function and Biology Details

Reaction catalysed:
Peptidylproline (omega=180) = peptidylproline (omega=0)
Biochemical function:
  • not assigned
Biological process:
Cellular component:
  • not assigned

Structure analysis Details

Assembly composition:
homo trimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-141661 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Trigger factor Chains: A, B, C
Molecule details ›
Chains: A, B, C
Length: 121 amino acids
Theoretical weight: 13.5 KDa
Source organism: Escherichia coli
Expression system: Escherichia coli
UniProt:
  • Canonical: P0A850 (Residues: 1-118; Coverage: 27%)
Gene names: JW0426, b0436, tig
Sequence domains: Bacterial trigger factor protein (TF)
Structure domains: Trigger factor ribosome-binding domain

Ligands and Environments

1 modified residue:

Experiments and Validation Details

Entry percentile scores
X-ray source: EMBL/DESY, HAMBURG BEAMLINE BW7A
Spacegroup: R32
Unit cell:
a: 71.644Å b: 71.644Å c: 375.409Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.208 0.208 0.238
Expression system: Escherichia coli