› 1o9w

X-ray diffraction
1.65Å resolution

F17-aG lectin domain from Escherichia coli in complex with N-acetyl-glucosamine

Released:
DOI: 10.2210/pdb1o9w/pdb
PDB 1o9w coloured by chain and viewed from the front.
PDB 1o9w coloured by chain and viewed from the side.
PDB 1o9w coloured by chain and viewed from the top.
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:
Cellular component:
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 NAG 1 x NAG
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: EMBL/DESY, HAMBURG BEAMLINE X13
Spacegroup: P6122
Unit cell:
a: 42.329Å b: 42.329Å c: 268.714Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.211 0.211 0.242
Expression system: Escherichia coli BL21

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Citations

16 review citations

Extractable Bacterial Surface Proteins in Probiotic-Host Interaction.
do Carmo et al. (2018)
15 more