› 1ms5

X-ray diffraction
2Å resolution

Triclinic form of Trypanosoma cruzi trans-sialidase, soaked with N-acetylneuraminyl-a-2,3-thio-galactoside (NA-S-Gal)

Released:
DOI: 10.2210/pdb1ms5/pdb
PDB entry 1ms5 coloured by chain, front view.
PDB entry 1ms5 coloured by chain, side view.
PDB entry 1ms5 coloured by chain, top view.
Source organism: Trypanosoma cruzi
Primary publication:
The crystal structure and mode of action of trans-sialidase, a key enzyme in Trypanosoma cruzi pathogenesis.
Buschiazzo A, Amaya MF, Cremona ML, Frasch AC, Alzari PM
Mol Cell 10 757-68 (2002)
PMID: 12419220

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 Chains: A, B
Molecule details ›
Chains: A, B
Length: 648 amino acids
Theoretical weight: 71.4 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

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE ID14-1
Spacegroup: P1
Unit cell:
a: 51.365Å b: 74.692Å c: 88.074Å
α: 86° β: 84.2° γ: 88.38°
R-values:
R R work R free
0.173 0.17 0.237
Expression system: Escherichia coli

Quick links

Citations

19 review citations

Trypanosoma cruzi surface mucins: host-dependent coat diversity.
Buscaglia et al. (2006)
18 more

1 mention 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)