› 3ooe

X-ray diffraction
2Å resolution

Crystal structure of E. Coli purine nucleoside phosphorylase with PO4

Released:
DOI: 10.2210/pdb3ooe/pdb
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PDB entry 3ooe coloured by chain, front view.
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Source organism: Escherichia coli K-12
Primary publication:
Validation of the catalytic mechanism of Escherichia coli purine nucleoside phosphorylase by structural and kinetic studies.
Mikleušević G, Stefanić Z, Narczyk M, Wielgus-Kutrowska B, Bzowska A, Luić M
Biochimie 93 1610-22 (2011)
PMID: 21672603

Function and Biology Details

Reaction catalysed: 
Purine deoxynucleoside + phosphate = purine + 2'-deoxy-alpha-D-ribose 1-phosphate
Biochemical function:
Biological process:
Cellular component:
Sequence domains:

Structure analysis Details

Assembly composition:
homo hexamer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-142186 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Purine nucleoside phosphorylase DeoD-type Chains: A, B, C, D, E, F
Molecule details ›
Chains: A, B, C, D, E, F
Length: 237 amino acids
Theoretical weight: 25.72 KDa
Source organism: Escherichia coli K-12
Expression system: Escherichia coli
UniProt:
  • Canonical: P0ABP8 (Residues: 2-238; Coverage: 99%)
Gene names: JW4347, b4384, deoD, pup
Sequence domains: Phosphorylase superfamily
Structure domains: Nucleoside phosphorylase domain

Ligands and Environments

1 bound ligand:
Ligand PO4 14 x PO4
No modified residues

Experiments and Validation Details

wwPDB Validation report is not available for this entry.
X-ray source: ESRF BEAMLINE BM14
Spacegroup: P212121
Unit cell:
a: 62.076Å b: 123.435Å c: 189.85Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.155 0.15 0.196
Expression system: Escherichia coli

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Citations

22 citation in other articles

Recombinant purine nucleoside phosphorylases from thermophiles: preparation, properties and activity towards purine and pyrimidine nucleosides.
Zhou et al. (2013)
21 more

1 mention without citation

Molecular replacement with a large number of molecules in the asymmetric unit.
Jobichen et al. (2014)

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