Zebisch Matthias, Schäfer Petra, Lauble Peter, Sträter Norbert
Institute of Bioanalytical Chemistry, Center for Biotechnology and Biomedicine, University of Leipzig, Deutscher Platz 5, 04103 Leipzig, Germany.
Acta Crystallogr Sect F Struct Biol Cryst Commun. 2013 Mar 1;69(Pt 3):257-62. doi: 10.1107/S1744309113001504. Epub 2013 Feb 22.
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.
核苷三磷酸二磷酸水解酶（NTPDases）是一大类核苷酸酶，它们分别水解核苷三磷酸和二磷酸的（γ/β）-和（β/α）-酐键。NTPDases存在于整个真核生物域中。此外，在细菌中也发现了极少数成员，其中大多数以真核宿主的寄生虫形式存在。细胞内和细胞外寄生虫的NTPDases正在成为寄生虫生存的重要调节因子。为了加深对这类酶的结构和功能的了解，已建立了从嗜肺军团菌中重组生产NTPDase1的方法。该蛋白质可以结晶成六种晶体形式，其中一种先前已有描述。这些晶体的衍射分辨率在
