› 6gty

X-ray diffraction
1.9Å resolution

Crystal structure of the FimH lectin domain from E.coli K12 in complex with the dimannoside Man(alpha1-6)Man

Released:
DOI: 10.2210/pdb6gty/pdb
PDB entry 6gty coloured by chain, front view.
PDB entry 6gty coloured by chain, side view.
PDB entry 6gty coloured by chain, top view.
Source organism: Escherichia coli K-12
Primary publication:
Binding of the Bacterial Adhesin FimH to Its Natural, Multivalent High-Mannose Type Glycan Targets.
Sauer MM, Jakob RP, Luber T, Canonica F, Navarra G, Ernst B, Unverzagt C, Maier T, Glockshuber R
J Am Chem Soc 141 936-944 (2019)
PMID: 30543411

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-140004 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecules (2 distinct):
Type 1 fimbrin D-mannose specific adhesin Chains: A, B, C, D, E
Molecule details ›
Chains: A, B, C, D, E
Length: 158 amino acids
Theoretical weight: 16.92 KDa
Source organism: Escherichia coli K-12
Expression system: Escherichia coli
UniProt:
  • Canonical: P08191 (Residues: 22-179; Coverage: 57%)
Gene names: JW4283, b4320, fimH
Sequence domains: FimH, mannose binding
Structure domains: Fimbrial-type adhesion domain

Ligands and Environments

Carbohydrate polymer : NEW Components: MMA, MAN
Carbohydrate polymer
No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SLS BEAMLINE X10SA
Spacegroup: P43
Unit cell:
a: 90.61Å b: 90.61Å c: 91.53Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.184 0.182 0.216
Expression system: Escherichia coli

Quick links

Citations

4 review citations

Urinary tract infections: microbial pathogenesis, host-pathogen interactions and new treatment strategies.
Klein et al. (2020)
3 more

2 mentions without citation

RMSD analysis of structures of the bacterial protein FimH identifies five conformations of its lectin domain.
Magala et al. (2020)
1 more