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.

中文翻译：

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大戟（Euphorbia characias）乳胶的核苷酸焦磷酸酶/磷酸二酯酶（NPP）的结构，其特征在于小角度X射线散射：是植物NPP总体组织的线索。

关于植物来源的核苷酸焦磷酸酶/磷酸二酯酶（NPPs）的结构特征，几乎没有信息，这些蛋白质的晶体结构尚未见报道。这项研究的目的是通过对地中海灌木大戟属乳胶中NPP的两个不同片段的序列进行比较分析来获得对这些方面的了解。（ELNPP）并通过小角度X射线散射研究溶液中纯化蛋白的低分辨率结构。这是迄今为止已报道的溶液中工厂NPP的第一个结构。结果表明，ELNPP序列在许多其他植物物种中高度保守。值得注意的是，这些植物NPP的催化结构域与哺乳动物NPP具有相同的高度保守的PDE结构域。此外，ELNPP是溶液中的二聚体，这种低聚状态很可能是其他植物酶所共有的。