ArticleProceedings of the National Academy of Sciences of the United States of America2008
Structural insight into signal conversion and inactivation by NTPDase2 in purinergic signaling.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 34 papers.
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34 citing papers in PubMed, 80 citations in OpenAlex.
- 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
- Heterologous expression and biochemical characterization of the recombinant nucleoside triphosphate diphosphohydrolase 2 (LbNTPDase2) from Leishmania (Viannia) braziliensis.Purinergic signalling · 2024Article
- Synthesis of new non-natural L-glycosidic flavonoid derivatives and their evaluation as inhibitors of Trypanosoma cruzi ecto-nucleoside triphosphate diphosphohydrolase 1 (TcNTPDase1).Purinergic signalling · 2024Article
- Synthesis and biological evaluation of sulfamoyl benzamide derivatives as selective inhibitors forRSC advances · 2023Article
- Effect of Thiazolidin-4-one Against Lipopolysaccharide-Induced Oxidative Damage, and Alterations in Adenine Nucleotide Hydrolysis and Acetylcholinesterase Activity in Cultured Astrocytes.Cellular and molecular neurobiology · 2023Article
- Overexpression ofInternational journal of molecular sciences · 2022Article
- Identification of Asiaticoside fromPharmaceutics · 2022Article
- ENTPD5: identification of splicing variants and their impact on cancer survival.Purinergic signalling · 2021Article
- Recent Advances Clarifying the Structure and Function of Plant Apyrases (Nucleoside Triphosphate Diphosphohydrolases).International journal of molecular sciences · 2021Review
- Ectonucleoside triphosphate diphosphohydrolases and ecto-5'-nucleotidase in purinergic signaling: how the field developed and where we are now.Purinergic signalling · 2021Review
- Crystal structure of the nucleotide-metabolizing enzyme NTPDase4.Protein science : a publication of the Protein Society · 2020Article
- Molecular dynamic simulations reveal structural insights into substrate and inhibitor binding modes and functionality of Ecto-Nucleoside Triphosphate Diphosphohydrolases.Scientific reports · 2018Article
- Various N-glycoforms differentially upregulate E-NTPDase activity of the NTPDase3/CD39L3 ecto-enzymatic domain.Purinergic signalling · 2017Article
- Structures and kinetics for plant nucleoside triphosphate diphosphohydrolases support a domain motion catalytic mechanism.Protein science : a publication of the Protein Society · 2017Article
- Mycobacterium tuberculosis proteasomal ATPase Mpa has a β-grasp domain that hinders docking with the proteasome core protease.Molecular microbiology · 2017Article
- Article
- The ENTPD5/mt-PCPH oncoprotein is a catalytically inactive member of the ectonucleoside triphosphate diphosphohydrolase family.International journal of oncology · 2013Article
- Mutagenesis of apyrase conserved region 1 alters the nucleotide substrate specificity.Plant signaling & behavior · 2013Article
- New crystal forms of NTPDase1 from the bacterium Legionella pneumophila.Acta crystallographica. Section F, Structural biology and crystallization communications · 2013Article
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2 authors at 1 institution in 1 country.
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No grant is acknowledged in the PubMed record.
Abstract
Cell surface-located nucleoside triphosphate diphosphohydrolases (NTPDase1, -2, -3, and -8) are oligomeric integral membrane proteins responsible for signal conversion and inactivation in extracellular nucleotide-mediated "purinergic" signaling. They catalyze the sequential hydrolysis of the signaling molecule ATP via ADP to AMP. Here we present the structure of the extracellular domain of Rattus norvegicus NTPDase2 in an active state at resolutions between 1.7 A and 2.1 A in four different forms: (i) apo form, (ii) ternary complex with the nonhydrolyzable ATP analog AMPPNP and cofactor Ca(2+), (iii) quaternary complex with Ca(2+) and bound products AMP and phosphate, and (iv) binary product complex with AMP only. Analysis of the ATP (analog) binding mode explains the importance of several residues for activity and allows suggestion of a catalytic mechanism. The carboxylate group of E165 serves as a catalytic base and activates a water molecule, which is well positioned for nucleophilic attack on the terminal phosphate. Based on analysis of the two product complex structures in which AMP adopts different conformations, a substrate binding mode for ADP hydrolysis is proposed. This allows for an understanding of how the same hydrolytic site can be engaged in ATP and ADP but not AMP hydrolysis.
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