ArticleProtein science : a publication of the Protein Society2017
Structures and kinetics for plant nucleoside triphosphate diphosphohydrolases support a domain motion catalytic mechanism.
Article in Protein science : a publication of the Protein Society, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.
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Who cites it
9 citing papers in PubMed.
- Levels of extracellular ATP in growth zones of Arabidopsis primary roots are changed by altered expression of apyrase enzymes.Plant signaling & behavior · 2025Article
- Structural Modeling of NTPDase-Substrate Complexes Preserving Catalytic Experimental Features.ACS omega · 2025Article
- Apyrase in horticultural crops: insights into growth, stress adaptation and quality regulation.Molecular horticulture · 2025Review
- Modified pea apyrase has altered nuclear functions and enhances the growth of yeast and Arabidopsis.Frontiers in plant science · 2025Article
- New Horizons in Plant Cell Signaling.International journal of molecular sciences · 2022Article
- Phosphate-deprivation and damage signalling by extracellular ATP.Frontiers in plant science · 2022Article
- Recent Advances Clarifying the Structure and Function of Plant Apyrases (Nucleoside Triphosphate Diphosphohydrolases).International journal of molecular sciences · 2021Review
- Crystal structure of the nucleotide-metabolizing enzyme NTPDase4.Protein science : a publication of the Protein Society · 2020Article
- Intracellular parasitism, the driving force of evolution of Legionella pneumophila and the genus Legionella.Genes and immunity · 2019Review
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5 authors.
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No grant is acknowledged in the PubMed record.
Abstract
Extracellular nucleoside triphosphate diphosphohydrolases (NTPDases) are enzymes that hydrolyze extracellular nucleotides to the respective monophosphate nucleotides. In the past 20 years, NTPDases belonging to mammalian, parasitic and prokaryotic domains of life have been discovered, cloned and characterized. We reveal the first structures of NTPDases from the legume plant species Trifolium repens (7WC) and Vigna unguiculata subsp. cylindrica (DbLNP). Four crystal structures of 7WC and DbLNP were determined at resolutions between 1.9 and 2.6 Å. For 7WC, structures were determined for an -apo form (1.89 Å) and with the product AMP (2.15 Å) and adenine and phosphate (1.76 Å) bound. For DbLNP, a structure was solved with phosphate and manganese bound (2.60 Å). Thorough kinetic data and analysis is presented. The structure of 7WC and DbLNP reveals that these NTPDases can adopt two conformations depending on the molecule and co-factor bound in the active site. A central hinge region creates a "butterfly-like" motion of the domains that reduces the width of the inter-domain active site cleft upon molecule binding. This phenomenon has been previously described in Rattus norvegicus and Legionella pneumophila NTPDaseI and Toxoplasma gondii NTPDaseIII suggesting a common catalytic mechanism across the domains of life.
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