Institute of Bioanalytical Chemistry, Faculty of Chemistry and Mineralogy, Center for Biotechnology and Biomedicine, University of Leipzig, 04103 Leipzig, Germany.
Proteins. 2013 Jul;81(7):1271-6. doi: 10.1002/prot.24288. Epub 2013 Apr 20.
Toxoplasma gondii nucleoside triphosphate diphosphohydrolase (NTPDase) 1 was crystallized in an intermediate tetrameric conformation. The crystal structure is similar to that of T. gondii NTPDase3 and represents an inactive conformation as the activating disulfide bridge is not reduced and the active site cleft between the two domains of each monomer is open. However, the arrangement of the monomers within the tetramer differs from that of the inactive form of NTPDase3 and may represent an intermediate conformation on the path of the closure motion of the tetramer induced upon activation.
刚地弓形虫核苷三磷酸二磷酸水解酶（NTPDase）1 以中间四聚体构象结晶。晶体结构与刚地弓形虫 NTPDase3 相似，代表一种无活性构象，因为激活的二硫键未还原，并且每个单体的两个结构域之间的活性位点裂隙是打开的。然而，四聚体中单体的排列与 NTPDase3 的无活性形式不同，可能代表在激活诱导的四聚体闭合运动过程中的中间构象。
