State Key Laboratory of Silkworm Genome Biology, College of Biotechnology, Southwest University, Beibei, Chongqing, 400715, China.
Institute of Medical Research, Northwestern Polytechnical University, Xi'an, Shaan Xi, 710072, China.
Sci Rep. 2020 Feb 21;10(1):3195. doi: 10.1038/s41598-020-60263-4.
Deciphering the activity-conformation relationship of PTPase is of great interest to understand how PTPase activity is determined by its conformation. Here we studied the activity and conformational transitions of PTPase from thermus thermophilus HB27 in the presence of sodium dodecyl sulfate (SDS). Activity assays showed the inactivation of PTPase induced by SDS was in a concentration-dependent manner. Fluorescence and circular dichroism spectra suggested SDS induced significant conformational transitions of PTPase, which resulted in the inactivation of PTPase, and the changes of α-helical structure and tertiary structure of PTPase. Structural analysis revealed a number of hydrophobic and charged residues around the active sites of PTPase may be involved in the hydrophobic and ionic bonds interactions of PTPase and SDS, which are suggested to be the major driving force to result in PTPase inactivation and conformational transitions induced by SDS. Our results suggested the hydrophobic and charged residues around the active sites were essential for the activity and conformation of PTPase. Our study promotes a better understanding of the activity and conformation of PTPase.
解析 PTPase 的活性构象关系对于理解 PTPase 活性如何由其构象决定具有重要意义。在这里，我们研究了在十二烷基硫酸钠 (SDS) 存在下来自嗜热栖热菌 HB27 的 PTPase 的活性和构象转变。活性测定表明，SDS 诱导的 PTPase 失活呈浓度依赖性。荧光和圆二色光谱表明，SDS 诱导了 PTPase 的显著构象转变，导致 PTPase 失活，并改变了 PTPase 的α-螺旋结构和三级结构。结构分析表明，PTPase 活性位点周围的一些疏水和带电残基可能参与 PTPase 和 SDS 之间的疏水和离子键相互作用，这被认为是导致 PTPase 失活和 SDS 诱导的构象转变的主要驱动力。我们的结果表明，活性位点周围的疏水和带电残基对于 PTPase 的活性和构象至关重要。我们的研究促进了对 PTPase 活性和构象的更好理解。
