State Key Laboratory of Virology, Department of Biochemistry and Molecular Biology, College of Life Sciences, Wuhan University, Wuhan, PR China.
FEBS Lett. 2010 Dec 1;584(23):4789-96. doi: 10.1016/j.febslet.2010.11.011. Epub 2010 Nov 11.
Here, we show that during in vivo folding of the precursor, the propeptide of subtilisin nattokinase functions as an intramolecular chaperone (IMC) that organises the in vivo folding of the subtilisin domain. Two residues belonging to β-strands formed by conserved regions of the IMC are crucial for the folding of the subtilisin domain through direct interactions. An identical protease can fold into different conformations in vivo due to the action of a mutated IMC, resulting in different kinetic parameters. Some interfacial changes involving conserved regions, even those induced by the subtilisin domain, blocked subtilisin folding and altered its conformation. Insight into the interaction between the subtilisin and IMC domains is provided by a three-dimensional structural model.
在这里，我们表明，在原酶前体的体内折叠过程中，纳豆激酶原肽作为一种分子内伴侣（IMC）发挥作用，组织了枯草杆菌蛋白酶结构域的体内折叠。属于 IMC 保守区域形成的β-折叠的两个残基对于通过直接相互作用折叠枯草杆菌蛋白酶结构域是至关重要的。由于突变的 IMC 的作用，相同的蛋白酶可以在体内折叠成不同的构象，从而导致不同的动力学参数。涉及保守区域的一些界面变化，甚至是由枯草杆菌蛋白酶结构域诱导的变化，也会阻止枯草杆菌蛋白酶的折叠并改变其构象。通过三维结构模型提供了对枯草杆菌蛋白酶和 IMC 结构域之间相互作用的深入了解。
