ArticleActa crystallographica. Section F, Structural biology communications2016
X-ray crystallographic studies of the extracellular domain of the first plant ATP receptor, DORN1, and the orthologous protein from Camelina sativa.
Article in Acta crystallographica. Section F, Structural biology communications, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.
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Who cites it
8 citing papers in PubMed, 16 citations in OpenAlex.
- The intrinsically disordered C-terminus of purinoceptor P2K1 fine-tunes plant responses to extracellular ATP.FEBS letters · 2023Article
- Knowing me, knowing you: Self and non-self recognition in plant immunity.Essays in biochemistry · 2022Article
- Genome-wide identification and functional exploration of the legume lectin genes inFrontiers in plant science · 2022Article
- Phosphate-deprivation and damage signalling by extracellular ATP.Frontiers in plant science · 2022Article
- DORN1/P2K1 and purino-calcium signalling in plants: making waves with extracellular ATP.Annals of botany · 2020Article
- Purinoceptor P2K1/DORN1 Enhances Plant Resistance Against a Soilborne Fungal Pathogen,Frontiers in plant science · 2020Article
- Modifying Baculovirus Expression Vectors to Produce Secreted Plant Proteins in Insect Cells.Journal of visualized experiments : JoVE · 2018Article
- Plant Lectins and Lectin Receptor-Like Kinases: How Do They Sense the Outside?International journal of molecular sciences · 2017Review
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
Abstract
Does not respond to nucleotides 1 (DORN1) has recently been identified as the first membrane-integral plant ATP receptor, which is required for ATP-induced calcium response, mitogen-activated protein kinase activation and defense responses in Arabidopsis thaliana. In order to understand DORN1-mediated ATP sensing and signal transduction, crystallization and preliminary X-ray studies were conducted on the extracellular domain of DORN1 (atDORN1-ECD) and that of an orthologous protein, Camelina sativa lectin receptor kinase I.9 (csLecRK-I.9-ECD or csI.9-ECD). A variety of deglycosylation strategies were employed to optimize the glycosylated recombinant atDORN1-ECD for crystallization. In addition, the glycosylated csI.9-ECD protein was crystallized at 291 K. X-ray diffraction data were collected at 4.6 Å resolution from a single crystal. The crystal belonged to space group C222 or C222
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