X-ray diffraction
2.15Å resolution

Ribosome binding of E. coli Trigger Factor mutant F44L.

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:
monomeric (preferred)
Entry contents:
1 distinct polypeptide molecule
Trigger factor Chains: A, B
Molecule details ›
Chains: A, B
Length: 121 amino acids
Theoretical weight: 13.33 KDa
Source organism: Escherichia coli
Expression system: Escherichia coli BL21(DE3)
  • Canonical: P0A850 (Residues: 1-118; Coverage: 27%)
Gene names: JW0426, b0436, tig
Structure domains: Trigger factor ribosome-binding domain

Ligands and Environments

1 bound ligand:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: MAX II BEAMLINE I711
Spacegroup: R32
Unit cell:
a: 71.901Å b: 71.901Å c: 257.659Å
α: 90° β: 90° γ: 120°
R R work R free
0.2 0.2 0.247
Expression system: Escherichia coli BL21(DE3)