› 5o7u

X-ray diffraction
1.15Å resolution

Crystal structure of the 7-Fluorotryptophan RSL lectin in complex with Lewis x tetrasaccharide

Released:
DOI: 10.2210/pdb5o7u/pdb
PDB entry 5o7u coloured by chain, front view.
PDB entry 5o7u coloured by chain, side view.
PDB entry 5o7u coloured by chain, top view.
Source organism: Ralstonia solanacearum
Primary publication:
Effect of Noncanonical Amino Acids on Protein-Carbohydrate Interactions: Structure, Dynamics, and Carbohydrate Affinity of a Lectin Engineered with Fluorinated Tryptophan Analogs.
Tobola F, Lelimousin M, Varrot A, Gillon E, Darnhofer B, Blixt O, Birner-Gruenberger R, Imberty A, Wiltschi B
ACS Chem Biol 13 2211-2219 (2018)
PMID: 29812892

Function and Biology Details

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

Structure analysis Details

Assembly composition:
homo trimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-102700 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecules (5 distinct):
Fucose-binding lectin protein Chains: A, B
Molecule details ›
Chains: A, B
Length: 90 amino acids
Theoretical weight: 9.86 KDa
Source organism: Ralstonia solanacearum
Expression system: Escherichia coli
UniProt:
  • Canonical: A0A0S4TLR1 (Residues: 2-91; Coverage: 99%)
Gene names: E7Z57_08365, HF909_06975, LBW55_09125, RUN39_v1_50103
Sequence domains: Fungal fucose-specific lectin
Structure domains: Lipocalin

Ligands and Environments

Carbohydrate polymer : NEW Components: NAG, FUC, GAL
Carbohydrate polymer
Carbohydrate polymer : NEW Components: NAG, FUC, GAL, GLA
Carbohydrate polymer
Carbohydrate polymer : NEW Components: NAG, FUC
Carbohydrate polymer
Carbohydrate polymer : NEW Components: NAG, FUC, GAL
Carbohydrate polymer
2 bound ligands:
Ligand MG 2 x MG
Ligand CA 1 x CA
1 modified residue:
Ligand F7W 14 x F7W

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE BM30A
Spacegroup: F23
Unit cell:
a: 129.152Å b: 129.152Å c: 129.152Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.105 0.104 0.129
Expression system: Escherichia coli

Quick links

Citations

7 citation in other articles

What does fluorine do to a protein? Thermodynamic, and highly-resolved structural insights into fluorine-labelled variants of the cold shock protein.
Welte et al. (2020)
6 more

2 mentions without citation

Effect of Noncanonical Amino Acids on Protein-Carbohydrate Interactions: Structure, Dynamics, and Carbohydrate Affinity of a Lectin Engineered with Fluorinated Tryptophan Analogs.
Tobola et al. (2018)
1 more