› 4txj

X-ray diffraction
1.66Å resolution

Crystal structure of uridine phosphorylase from Schistosoma mansoni in complex with thymidine

Released:
DOI: 10.2210/pdb4txj/pdb
PDB entry 4txj coloured by chain, front view.
PDB entry 4txj coloured by chain, side view.
PDB entry 4txj coloured by chain, top view.
Source organism: Schistosoma mansoni
Primary publication:
Analysis of two Schistosoma mansoni uridine phosphorylases isoforms suggests the emergence of a protein with a non-canonical function.
da Silva Neto AM, Torini de Souza JR, Romanello L, Cassago A, Serrão VH, DeMarco R, Brandão-Neto J, Garratt RC, Pereira HD
Biochimie 125 12-22 (2016)
PMID: 26898674

Function and Biology Details

Reaction catalysed: 
Uridine + phosphate = uracil + alpha-D-ribose 1-phosphate
Biochemical function:
Biological process:
Cellular component:
Sequence domains:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-124459 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Uridine phosphorylase A Chains: A, B, C, D
Molecule details ›
Chains: A, B, C, D
Length: 296 amino acids
Theoretical weight: 32.65 KDa
Source organism: Schistosoma mansoni
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: G4VGI0 (Residues: 1-296; Coverage: 100%)
Gene names: Smp_082430, UPPA
Sequence domains: Phosphorylase superfamily
Structure domains: Nucleoside phosphorylase domain

Ligands and Environments

2 bound ligands:
Ligand THM 4 x THM
Ligand SO4 4 x SO4
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: DIAMOND BEAMLINE I04
Spacegroup: P212121
Unit cell:
a: 95.82Å b: 108.08Å c: 116.06Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.187 0.186 0.211
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

1 review citation

Pyrimidine metabolism in schistosomes: A comparison with other parasites and the search for potential chemotherapeutic targets.
El Kouni MH. (2017)
4 other articles

1 mention without citation

Strained Conformations of Nucleosides in Active Sites of Nucleoside Phosphorylases.
Il'icheva et al. (2020)