› 2a75

X-ray diffraction
1.95Å resolution

Trypanosoma rangeli Sialidase In Complex With 2,3- Difluorosialic Acid (Covalent Intermediate)

Released:
DOI: 10.2210/pdb2a75/pdb
PDB entry 2a75 coloured by chain, front view.
PDB entry 2a75 coloured by chain, side view.
PDB entry 2a75 coloured by chain, top view.
Source organism: Trypanosoma rangeli
Primary publication:
Structural and kinetic analysis of two covalent sialosyl-enzyme intermediates on Trypanosoma rangeli sialidase.
Watts AG, Oppezzo P, Withers SG, Alzari PM, Buschiazzo A
J Biol Chem 281 4149-55 (2006)
PMID: 16298994

Function and Biology Details

Reaction catalysed: 
Hydrolysis of alpha-(2->3)-, alpha-(2->6)-, alpha-(2->8)- glycosidic linkages of terminal sialic acid residues in oligosaccharides, glycoproteins, glycolipids, colominic acid and synthetic substrates.
Biochemical function:
Biological process:
Cellular component:
Sequence domains:
Structure domains:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-129183 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Sialidase domain-containing protein Chain: A
Molecule details ›
Chain: A
Length: 652 amino acids
Theoretical weight: 71.21 KDa
Source organism: Trypanosoma rangeli
Expression system: Escherichia coli
UniProt:
  • Canonical: O44049 (Residues: 23-660; Coverage: 100%)
Sequence domains: BNR repeat-like domain
Structure domains:

Ligands and Environments

2 bound ligands:
Ligand SO4 2 x SO4
Ligand FSI 1 x FSI
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE ID29
Spacegroup: P212121
Unit cell:
a: 74.218Å b: 96.102Å c: 106.648Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.174 0.174 0.216
Expression system: Escherichia coli

Quick links

Citations

8 review citations

Mechanistic insights into glycosidase chemistry.
Vocadlo et al. (2008)
7 more

4 mentions without citation

Modulation of catalytic function by differential plasticity of the active site: case study of Trypanosoma cruzi trans-sialidase and Trypanosoma rangeli sialidase.
Demir et al. (2009)
3 more