› 1s0j

X-ray diffraction
1.65Å resolution

Trypanosoma cruzi trans-sialidase in complex with MuNANA (Michaelis complex)

Released:
DOI: 10.2210/pdb1s0j/pdb
PDB entry 1s0j coloured by chain, front view.
PDB entry 1s0j coloured by chain, side view.
PDB entry 1s0j coloured by chain, top view.
Source organism: Trypanosoma cruzi
Primary publication:
Structural insights into the catalytic mechanism of Trypanosoma cruzi trans-sialidase.
Amaya MF, Watts AG, Damager I, Wehenkel A, Nguyen T, Buschiazzo A, Paris G, Frasch AC, Withers SG, Alzari PM
Structure 12 775-84 (2004)
PMID: 15130470

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-173256 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Sialidase domain-containing protein Chain: A
Molecule details ›
Chain: A
Length: 648 amino acids
Theoretical weight: 71.35 KDa
Source organism: Trypanosoma cruzi
Expression system: Escherichia coli
UniProt:
  • Canonical: Q26966 (Residues: 2-635; Coverage: 99%)
Sequence domains: BNR repeat-like domain
Structure domains:

Ligands and Environments

1 bound ligand:
Ligand MUS 1 x MUS
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE ID14-2
Spacegroup: P21
Unit cell:
a: 54.373Å b: 129.423Å c: 54.234Å
α: 90° β: 108.33° γ: 90°
R-values:
R R work R free
0.163 0.162 0.194
Expression system: Escherichia coli

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Citations

19 review citations

Advances in the biology and chemistry of sialic acids.
Chen et al. (2010)
18 more

6 mentions without citation

The Potential of Secondary Metabolites from Plants as Drugs or Leads against Protozoan Neglected Diseases-Part III: In-Silico Molecular Docking Investigations.
Ogungbe et al. (2016)
5 more