ArticleThe Journal of biological chemistry2012
Structural insight into activation mechanism of Toxoplasma gondii nucleoside triphosphate diphosphohydrolases by disulfide reduction.
Article in The Journal of biological chemistry, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.
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Who cites it
13 citing papers in PubMed, 25 citations in OpenAlex.
- Genetically encoded manipulation of ATP/ADP ratio in human cells uncovers proteomic and physiological signatures of energy stress.Cell chemical biology · 2026Article
- Design, synthesis, and enzyme kinetic evaluation of oxadiazole derivatives as nucleoside triphosphate diphosphohydrolase (NTPDase) inhibitors: an integratedRSC advances · 2026Article
- Structural Modeling of NTPDase-Substrate Complexes Preserving Catalytic Experimental Features.ACS omega · 2025Article
- Lucidin fromPharmaceuticals (Basel, Switzerland) · 2025Article
- Heterologous expression and biochemical characterization of the recombinant nucleoside triphosphate diphosphohydrolase 2 (LbNTPDase2) from Leishmania (Viannia) braziliensis.Purinergic signalling · 2024Article
- Crystal structure of the nucleotide-metabolizing enzyme NTPDase4.Protein science : a publication of the Protein Society · 2020Article
- Establishment of Novel High-Standard Chemiluminescent Assay for NTPase in Two Protozoans and Its High-Throughput Screening.Marine drugs · 2020Article
- Review
- Structures and kinetics for plant nucleoside triphosphate diphosphohydrolases support a domain motion catalytic mechanism.Protein science : a publication of the Protein Society · 2017Article
- The tandemly repeated NTPase (NTPDase) from Neospora caninum is a canonical dense granule protein whose RNA expression, protein secretion and phosphorylation coincides with the tachyzoite egress.Parasites & vectors · 2016Article
- Article
- New crystal forms of NTPDase1 from the bacterium Legionella pneumophila.Acta crystallographica. Section F, Structural biology and crystallization communications · 2013Article
- Cellular function and molecular structure of ecto-nucleotidases.Purinergic signalling · 2012Review
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The intracellular parasite Toxoplasma gondii produces two nucleoside triphosphate diphosphohydrolases (NTPDase1 and -3). These tetrameric, cysteine-rich enzymes require activation by reductive cleavage of a hitherto unknown disulfide bond. Despite a 97% sequence identity, both isozymes differ largely in their ability to hydrolyze ATP and ADP. Here, we present crystal structures of inactive NTPDase3 as an apo form and in complex with the product AMP to resolutions of 2.0 and 2.2 Å, respectively. We find that the enzyme is present in an open conformation that precludes productive substrate binding and catalysis. The cysteine bridge 258-268 is identified to be responsible for locking of activity. Crystal structures of constitutively active variants of NTPDase1 and -3 generated by mutation of Cys(258)-Cys(268) show that opening of the regulatory cysteine bridge induces a pronounced contraction of the whole tetramer. This is accompanied by a 12° domain closure motion resulting in the correct arrangement of all active site residues. A complex structure of activated NTPDase3 with a non-hydrolyzable ATP analog and the cofactor Mg(2+) to a resolution of 2.85 Å indicates that catalytic differences between the NTPDases are primarily dictated by differences in positioning of the adenine base caused by substitution of Arg(492) and Glu(493) in NTPDase1 by glycines in NTPDase3.
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