摘要
封面上展示的是活性降解26S蛋白酶体的结构,显示出腺苷三磷酸酶(ATP酶)马达的连续状态与守恒的酪氨酸桨(图中蓝色、绿色和黄色集群)以螺旋阶梯式排列,并将蛋白质基质(图中黄色块状物)拉进一个降解室。原始构象态是透明的,而后续的构象态是不透明的。这些数据为我们提供了一个机会深入了解这一AAA+家族成员是如何结合ATP水解与构象变化从而产生机械功的。
Structures of the actively degrading 26S proteasome show consecutive states of the ATPase motor with conserved tyrosine paddles(blue,green,and yellow clusters)arranged in a spiral staircase and pulling a protein substrate(yellow blocks)into a degradation chamber.Theoriginal conformational state is transparent,whereas the subsequent state is opaque.The data provide insights into how this member of the AAA+family couples ATP hydrolysis with conformational changes to produce mechanical work.
出处
《中国科技教育》
2019年第1期47-47,共1页
China Science & Technology Education