Proteomics

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Nucleotide pyrophosphatase/phosphodiesterase from Euphorbia characias latex

ABSTRACT: The low-resolution structure of a nucleotide pyrophosphatase/phosphodiesterase from Euphorbia characias latex (ELNPP) has been determined in solution by means of Small Angle X-ray Scattering (SAXS). To improve the structural resolution of ELNPP a partial sequencing after proteolytic cleavage of the protein was performed. Protein digestion followed by high-resolution HPLC-ESI-MS/MS analysis allowed us to identify two different peptides of 82 and 41 amino acids, respectively. These sequences exhibit a high degree of identity with other NPPs predicted sequences from several higher plants including Malus domestica, Morus notabilis, Ricinus communis, and Triticum aestivum. In particular, Triticum aestivum NPP is the protein with the highest identity level (98 identical positions) towards the obtained fragments of ELNPP. From the alignment with the entire sequence of TaNPP, the two obtained fragments contain some known conserved residues belonging to the catalytic domain of the mammalian NPP family enzymes.

INSTRUMENT(S): LTQ Orbitrap Elite

ORGANISM(S): Euphorbia Characias

TISSUE(S): Latex

SUBMITTER: Tiziana Cabras  

LAB HEAD: Tiziana Cabras

PROVIDER: PXD009976 | Pride | 2022-03-02

REPOSITORIES: Pride

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Dataset's files

Source:
Action DRS
ELNPP_Cagliari190416.raw Raw
Search_engine.prot_ELNNP.xml Xml
annotated_spectra_ELNNP.zip Other
peak_list_ELNNP.mgf Mgf
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Publications

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.

Sabatucci Annalaura A   Pintus Francesca F   Cabras Tiziana T   Vincenzoni Federica F   Maccarrone Mauro M   Medda Rosaria R   Dainese Enrico E  

Acta crystallographica. Section D, Structural biology 20200817 Pt 9

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 p  ...[more]

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