› 4auy

X-ray diffraction
2.1Å resolution

Structure of the FimH lectin domain in the trigonal space group, in complex with an hydroxyl propynyl phenyl alpha-D-mannoside at 2.1 A resolution

Released:
DOI: 10.2210/pdb4auy/pdb
PDB entry 4auy coloured by chain, front view.
PDB entry 4auy coloured by chain, side view.
PDB entry 4auy coloured by chain, top view.
Source organism: Escherichia coli UTI89
Primary publication:
The tyrosine gate as a potential entropic lever in the receptor-binding site of the bacterial adhesin FimH.
Wellens A, Lahmann M, Touaibia M, Vaucher J, Oscarson S, Roy R, Remaut H, Bouckaert J
Biochemistry 51 4790-9 (2012)
PMID: 22657089

Function and Biology Details

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

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Type 1 fimbrin D-mannose specific adhesin Chains: A, B
Molecule details ›
Chains: A, B
Length: 158 amino acids
Theoretical weight: 16.92 KDa
Source organism: Escherichia coli UTI89
Expression system: Escherichia coli BL21(DE3)
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

3 bound ligands:
Ligand HNW 2 x HNW
Ligand NI 2 x NI
Ligand SO4 2 x SO4
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SOLEIL BEAMLINE PROXIMA 1
Spacegroup: P3121
Unit cell:
a: 91.14Å b: 91.14Å c: 80.17Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.151 0.149 0.186
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

10 review citations

Biogenesis and adhesion of type 1 and P pili.
Lillington et al. (2014)
9 more

4 mentions without citation

Validation of Reactivity Descriptors to Assess the Aromatic Stacking within the Tyrosine Gate of FimH.
Roos et al. (2013)
3 more