› 3f65

X-ray diffraction
2.29Å resolution

The F4 fimbrial chaperone FaeE does not self-cap its interactive surfaces

Released:
DOI: 10.2210/pdb3f65/pdb
PDB entry 3f65 coloured by chain, front view.
PDB entry 3f65 coloured by chain, side view.
PDB entry 3f65 coloured by chain, top view.
Source organism: Escherichia coli
Primary publication:
The F4 fimbrial chaperone FaeE is stable as a monomer that does not require self-capping of its pilin-interactive surfaces.
Van Molle I, Moonens K, Buts L, Garcia-Pino A, Panjikar S, Wyns L, De Greve H, Bouckaert J
Acta Crystallogr D Biol Crystallogr 65 411-20 (2009)
PMID: 19390146

Function and Biology Details

Biochemical function:
  • not assigned
Biological process:
Cellular component:
Sequence domains:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-150459 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Chaperone protein FaeE Chains: A, B, C, D, E, F, G, H
Molecule details ›
Chains: A, B, C, D, E, F, G, H
Length: 224 amino acids
Theoretical weight: 24.8 KDa
Source organism: Escherichia coli
Expression system: Escherichia coli
UniProt:
  • Canonical: P25401 (Residues: 35-258; Coverage: 100%)
Gene name: faeE
Sequence domains: Pili and flagellar-assembly chaperone, PapD N-terminal domain
Structure domains: Immunoglobulins

Ligands and Environments

2 bound ligands:
Ligand MPD 3 x MPD
Ligand PO4 1 x PO4
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE ID14-1
Spacegroup: C2
Unit cell:
a: 195.689Å b: 78.491Å c: 184.567Å
α: 90° β: 102.15° γ: 90°
R-values:
R R work R free
0.224 0.224 0.26
Expression system: Escherichia coli

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Citations

2 review citations

Animal Enterotoxigenic Escherichia coli.
Dubreuil et al. (2016)
1 more