Structure of a nucleotide pyrophosphatase/phosphodiesterase (NPP) from Euphorbia characias latex characterized by small-angle X-ray scattering: Clues for the general organization of plant NPPs

Annalaura Sabatucci, Francesca Pintus, Tiziana Cabras, Federica Vincenzoni, Mauro MacCarrone, Rosaria Medda, Enrico Dainese

Research output: Contribution to journalArticlepeer-review

Abstract

Little information is available concerning the structural features of nucleotide pyrophosphatase/phosphodiesterases (NPPs) of plant origin and the crystal structures of these proteins have not yet been reported. The aim of this study was to obtain insight into these aspects by carrying out a comparative analysis of the sequences of two different fragments of an NPP from the latex of the Mediterranean shrub Euphorbia characias (ELNPP) and by studying the low-resolution structure of the purified protein in solution by means of small-angle X-ray scattering. This is the first structure of a plant NPP in solution that has been reported to date. It is shown that the ELNPP sequence is highly conserved in many other plant species. Of note, the catalytic domains of these plant NPPs have the same highly conserved PDE-domain organization as mammalian NPPs. Moreover, ELNPP is a dimer in solution and this oligomerization state is likely to be common to other plant enzymes.

Original languageEnglish
Pages (from-to)857-867
Number of pages11
JournalActa Crystallographica Section D: Structural Biology
Volume76
DOIs
Publication statusPublished - Sep 1 2020

Keywords

  • Catalytic domain spatial organization
  • Euphorbia characias
  • Nucleotide pyrophosphatase/phosphodiesterase
  • Primary-structure comparison
  • SAXS
  • Structure in solution

ASJC Scopus subject areas

  • Structural Biology

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