ArticleActa crystallographica. Section F, Structural biology and crystallization communications2013
New crystal forms of NTPDase1 from the bacterium Legionella pneumophila.
Article in Acta crystallographica. Section F, Structural biology and crystallization communications, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 papers.
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4 citing papers in PubMed, 13 citations in OpenAlex.
- X-ray transparent microfluidic platforms for membrane protein crystallization with microseeds.Lab on a chip · 2018Article
- Structures and kinetics for plant nucleoside triphosphate diphosphohydrolases support a domain motion catalytic mechanism.Protein science : a publication of the Protein Society · 2017Article
- Multiple Forms of Glutamate Dehydrogenase in Animals: Structural Determinants and Physiological Implications.Biology · 2016Review
- Article
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4 authors at 2 institutions in 3 countries.
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Abstract
Nucleoside triphosphate diphosphohydrolases (NTPDases) are a large class of nucleotidases that hydrolyze the (γ/β)- and (β/α)-anhydride bonds of nucleoside triphosphates and diphosphates, respectively. NTPDases are found throughout the eukaryotic domain. In addition, a very small number of members can be found in bacteria, most of which live as parasites of eukaryotic hosts. NTPDases of intracellular and extracellular parasites are emerging as important regulators for the survival of the parasite. To deepen the knowledge of the structure and function of this enzyme class, recombinant production of the NTPDase1 from the bacterium Legionella pneumophila has been established. The protein could be crystallized in six crystal forms, of which one has been described previously. The crystals diffracted to resolutions of between 1.4 and 2.5 Å. Experimental phases determined by a sulfur SAD experiment using an orthorhombic crystal form produced an interpretable electron-density map.
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