PDBsum entry 1v45

Transferase

PDB id: 1v45

Contents

Protein chain

288 a.a. *

Ligands

SO4 ×3

3DG

Waters ×30

* Residue conservation analysis

PDB id:

1v45

Name:

Transferase

Title:

Crystal structure of human pnp complexed with 3-deoxyguanosine

Structure:

Purine nucleoside phosphorylase. Chain: e. Synonym: inosine phosphorylase, pnp. Engineered: yes

Source:

Homo sapiens. Human. Organism_taxid: 9606. Expressed in: escherichia coli. Expression_system_taxid: 562.

Biol. unit:

Trimer (from PDB file)

Resolution:

2.86Å R-factor: 0.180 R-free: 0.249

Authors:

F.Canduri,D.M.Dos Santos,R.G.Silva,M.A.Mendes,M.S.Palma,W.F.De Azevedo Jr.,L.A.Basso,D.S.Santos

Key ref:

F.Canduri et al. (2005). Structure of human PNP complexed with ligands. Acta Crystallogr D Biol Crystallogr, 61, 856-862. PubMed id: 15983407 DOI: 10.1107/S0907444905005421

Date:

10-Nov-03 Release date: 14-Dec-04

Protein chain

P00491  (PNPH_HUMAN) -  Purine nucleoside phosphorylase from Homo sapiens

Seq: 289 a.a.

Struc: 288 a.a.*

* PDB and UniProt seqs differ at 1 residue position (black cross)

Enzyme reactions

• Enzyme class: E.C.2.4.2.1 - purine-nucleoside phosphorylase.
• Reaction:
  1. a purine D-ribonucleoside + phosphate = a purine nucleobase + alpha- D-ribose 1-phosphate
  2. a purine 2'-deoxy-D-ribonucleoside + phosphate = a purine nucleobase + 2-deoxy-alpha-D-ribose 1-phosphate

Molecule diagrams generated from .mol files obtained from the KEGG ftp site

reference

DOI no: 10.1107/S0907444905005421

Acta Crystallogr D Biol Crystallogr 61:856-862 (2005)

PubMed id: 15983407

Structure of human PNP complexed with ligands.

F.Canduri, R.G.Silva, D.M.dos Santos, M.S.Palma, L.A.Basso, D.S.Santos, W.F.de Azevedo.

ABSTRACT

Purine nucleoside phosphorylase (PNP) is a key enzyme in the purine-salvage pathway, which allows cells to utilize preformed bases and nucleosides in order to synthesize nucleotides. PNP is specific for purine nucleosides in the beta-configuration and exhibits a strong preference for purines containing a 6-keto group and ribosyl-containing nucleosides relative to the corresponding analogues. PNP was crystallized in complex with ligands and data collection was performed using synchrotron radiation. This work reports the structure of human PNP in complex with guanosine (at 2.80 A resolution), 3'-deoxyguanosine (at 2.86 A resolution) and 8-azaguanine (at 2.85 A resolution). These structures were compared with the PNP-guanine, PNP-inosine and PNP-immucillin-H complexes solved previously.

Selected figure(s)

Figure 3.
Figure 3 Superposition of PNP apoenzyme with the PNP-guanine complex, showing the gate movement, which involves a helical transformation of residues 257-265 in the transition apoenzyme complex. Movements of the residues Tyr249, His257 and Lys265 and the position of ligand and sulfates can be observed. The figure was generated with the program MOLMOL (Koradi et al., 1996[Koradi, R., Billeter, M. & Wuthrich, K. (1996). J. Mol. Graph. 14, 51-55.]).

Figure 4.
Figure 4 Binding site of human PNP. (a) HsPNP-guanosine, (b) HsPNP-inosine, (c) HsPNP-immucillin-H, (d) HsPNP-3'-deoxyguanosine, (e) HsPNP-8-azaguanine, (f) HsPNP-guanine.

The above figures are reprinted by permission from the IUCr: Acta Crystallogr D Biol Crystallogr (2005, 61, 856-862) copyright 2005.

Figures were selected by an automated process.