› 3gu0

X-ray diffraction
3.5Å resolution

Promiscuous Substrate Recognition in Folding and Assembly Activities of the Trigger Factor Chaperone

Released:
DOI: 10.2210/pdb3gu0/pdb
PDB entry 3gu0 coloured by chain, front view.
PDB entry 3gu0 coloured by chain, side view.
PDB entry 3gu0 coloured by chain, top view.
Source organism: Thermotoga maritima
Primary publication:
Promiscuous substrate recognition in folding and assembly activities of the trigger factor chaperone.
Martinez-Hackert E, Hendrickson WA
Cell 138 923-34 (2009)
PMID: 19737520

Function and Biology Details

Reaction catalysed: 
Peptidylproline (omega=180) = peptidylproline (omega=0)
Biochemical function:
Biological process:
Cellular component:
Sequence domains:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-194603 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Trigger factor Chain: A
Molecule details ›
Chain: A
Length: 412 amino acids
Theoretical weight: 48.79 KDa
Source organism: Thermotoga maritima
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: Q9WZF8 (Residues: 1-405; Coverage: 95%)
Gene names: TM_0694, tig
Sequence domains:
Structure domains:

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: NSLS BEAMLINE X4A
Spacegroup: C2221
Unit cell:
a: 95.387Å b: 114.487Å c: 94.558Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.25 0.244 0.358
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

25 review citations

Molecular chaperone functions in protein folding and proteostasis.
Kim et al. (2013)
24 more

4 mentions without citation

A growing toolbox of techniques for studying β-barrel outer membrane protein folding and biogenesis.
Horne et al. (2016)
3 more