› 2bsx

X-ray diffraction
2Å resolution

Crystal structure of the Plasmodium falciparum purine nucleoside phosphorylase complexed with inosine

Released:
DOI: 10.2210/pdb2bsx/pdb
PDB entry 2bsx coloured by chain, front view.
PDB entry 2bsx coloured by chain, side view.
PDB entry 2bsx coloured by chain, top view.
Source organism: Plasmodium falciparum 3D7
Primary publication:
Structures of Plasmodium falciparum purine nucleoside phosphorylase complexed with sulfate and its natural substrate inosine.
Schnick C, Robien MA, Brzozowski AM, Dodson EJ, Murshudov GN, Anderson L, Luft JR, Mehlin C, Hol WG, Brannigan JA, Wilkinson AJ
Acta Crystallogr D Biol Crystallogr 61 1245-54 (2005)
PMID: 16131758

Function and Biology Details

Reactions catalysed: 
Purine deoxynucleoside + phosphate = purine + 2'-deoxy-alpha-D-ribose 1-phosphate
S-methyl-5'-thioinosine + phosphate = hypoxanthine + S-methyl-5-thio-alpha-D-ribose 1-phosphate
Biochemical function:
Biological process:
Cellular component:
Sequence domains:
Structure domain:

Structure analysis Details

Assembly composition:
homo hexamer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-184666 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Purine nucleoside phosphorylase Chain: A
Molecule details ›
Chain: A
Length: 253 amino acids
Theoretical weight: 27.96 KDa
Source organism: Plasmodium falciparum 3D7
Expression system: Escherichia coli BL21
UniProt:
  • Canonical: Q8I3X4 (Residues: 1-245; Coverage: 100%)
Gene names: PF3D7_0513300, PNP
Sequence domains: Phosphorylase superfamily
Structure domains: Nucleoside phosphorylase domain

Ligands and Environments

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

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE ID29
Spacegroup: P321
Unit cell:
a: 95.117Å b: 95.117Å c: 47.075Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.268 0.264 0.342
Expression system: Escherichia coli BL21

Quick links

Citations

3 review citations

Targeting purine and pyrimidine metabolism in human apicomplexan parasites.
Hyde JE. (2007)
2 more

5 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)
4 more