› 1o9v

X-ray diffraction
1.75Å resolution

F17-aG lectin domain from Escherichia coli in complex with a selenium carbohydrate derivative

Released:
DOI: 10.2210/pdb1o9v/pdb
PDB entry 1o9v coloured by chain, front view.
PDB entry 1o9v coloured by chain, side view.
PDB entry 1o9v coloured by chain, top view.
Source organism: Escherichia coli
Primary publication:
The fimbrial adhesin F17-G of enterotoxigenic Escherichia coli has an immunoglobulin-like lectin domain that binds N-acetylglucosamine.
Buts L, Bouckaert J, De Genst E, Loris R, Oscarson S, Lahmann M, Messens J, Brosens E, Wyns L, De Greve H
Mol Microbiol 49 705-15 (2003)
PMID: 12864853

Function and Biology Details

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

Structure analysis Details

Assembly composition:
monomeric (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
F17a-G fimbrial adhesin Chain: A
Molecule details ›
Chain: A
Length: 177 amino acids
Theoretical weight: 19.05 KDa
Source organism: Escherichia coli
Expression system: Escherichia coli BL21
UniProt:
  • Canonical: Q99003 (Residues: 23-199; Coverage: 55%)
Gene name: f17aG
Sequence domains: Fimbrial adhesin F17-AG, lectin domain
Structure domains: Bacterial adhesins - F17c-type

Ligands and Environments

1 bound ligand:
Ligand SNG 1 x SNG
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: EMBL/DESY, HAMBURG BEAMLINE BW7A
Spacegroup: P6122
Unit cell:
a: 42.757Å b: 42.757Å c: 273.758Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.205 0.205 0.235
Expression system: Escherichia coli BL21

Quick links

Citations

17 review citations

Evolution of the chaperone/usher assembly pathway: fimbrial classification goes Greek.
Nuccio et al. (2007)
16 more