5I3C

Crystal structure of E.coli purine nucleoside phosphorylase with acycloguanosine


Experimental Data Snapshot

  • Method: X-RAY DIFFRACTION
  • Resolution: 2.32 Å
  • R-Value Free: 0.217 
  • R-Value Work: 0.176 
  • R-Value Observed: 0.178 

Starting Model: experimental
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This is version 2.1 of the entry. See complete history


Literature

Crystal structure of Escherichia coli purine nucleoside phosphorylase complexed with acyclovir.

Timofeev, V.I.Zhukhlistova, N.E.Abramchik, Y.A.Muravieva, T.I.Esipov, R.S.Kuranova, I.P.

(2018) Acta Crystallogr F Struct Biol Commun 74: 402-409

  • DOI: https://doi.org/10.1107/S2053230X18008087
  • Primary Citation of Related Structures:  
    5I3C

  • PubMed Abstract: 

    Escherichia coli purine nucleoside phosphorylase (PNP), which catalyzes the reversible phosphorolysis of purine ribonucleosides, belongs to the family I hexameric PNPs. Owing to their key role in the purine salvage pathway, PNPs are attractive targets for drug design against some pathogens. Acyclovir (ACV) is an acyclic derivative of the PNP substrate guanosine and is used as an antiviral drug for the treatment of some human viral infections. The crystalline complex of E. coli PNP with acyclovir was prepared by co-crystallization in microgravity using counter-diffusion through a gel layer in a capillary. The structure of the E. coli PNP-ACV complex was solved at 2.32 Å resolution using the molecular-replacement method. The ACV molecule is observed in two conformations and sulfate ions were located in both the nucleoside-binding and phosphate-binding pockets of the enzyme. A comparison with the complexes of other hexameric and trimeric PNPs with ACV shows the similarity in acyclovir binding by these enzymes.


  • Organizational Affiliation

    Shubnikov Institute of Crystallography, Federal Scientific Research Centre `Crystallography and Photonics' of Russian Academy of Sciences, Leninsky Prospekt 59, Moscow 119333, Russian Federation.


Macromolecules
Find similar proteins by:  (by identity cutoff)  |  3D Structure
Entity ID: 1
MoleculeChains Sequence LengthOrganismDetailsImage
Purine nucleoside phosphorylase DeoD-type
A, B, C
237Escherichia coli O139:H28 str. E24377AMutation(s): 0 
Gene Names: deoDEcE24377A_4983
EC: 2.4.2.1
UniProt
Find proteins for A7ZVS7 (Escherichia coli O139:H28 (strain E24377A / ETEC))
Explore A7ZVS7 
Go to UniProtKB:  A7ZVS7
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupA7ZVS7
Sequence Annotations
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  • Reference Sequence
Small Molecules
Ligands 2 Unique
IDChains Name / Formula / InChI Key2D Diagram3D Interactions
AC2
Query on AC2

Download Ideal Coordinates CCD File 
D [auth A],
F [auth B],
H [auth C]
9-HYROXYETHOXYMETHYLGUANINE
C8 H11 N5 O3
MKUXAQIIEYXACX-UHFFFAOYSA-N
SO4
Query on SO4

Download Ideal Coordinates CCD File 
E [auth A],
G [auth B],
I [auth C],
J [auth C],
K [auth C]
SULFATE ION
O4 S
QAOWNCQODCNURD-UHFFFAOYSA-L
Experimental Data & Validation

Experimental Data

  • Method: X-RAY DIFFRACTION
  • Resolution: 2.32 Å
  • R-Value Free: 0.217 
  • R-Value Work: 0.176 
  • R-Value Observed: 0.178 
  • Space Group: P 61 2 2
Unit Cell:
Length ( Å )Angle ( ˚ )
a = 120.03α = 90
b = 120.03β = 90
c = 238.141γ = 120
Software Package:
Software NamePurpose
REFMACrefinement
iMOSFLMdata reduction
SCALAdata scaling
PHASERphasing

Structure Validation

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Ligand Structure Quality Assessment 


Entry History 

Deposition Data

Revision History  (Full details and data files)

  • Version 1.0: 2017-02-22
    Type: Initial release
  • Version 2.0: 2018-07-11
    Changes: Atomic model, Data collection, Database references
  • Version 2.1: 2024-01-10
    Changes: Data collection, Database references, Refinement description