Mutation in the SH1 helix reduces the activation energy of the ATP-induced conformational transition of myosin.
Mutation in the SH1 helix reduces the activation energy of the ATP-induced conformational transition of myosin.
复制标题
SH1 螺旋的突变降低了 ATP 诱导的肌球蛋白构象转变的活化能。
DOI：
10.1016/j.bbrc.2007.03.155
复制
发表时间：
2007
影响因子：
3.1
通讯作者：
S. Chaen
中科院分区：
文献类型：
--
作者：
S. Iwai;S. Chaen
SH1螺旋是一个连接转换子域和肌球蛋白马达结构域其余部分的关节。最近，我们发现Dictyostelialmyosin II(R689H)的SH1螺旋内的一个突变降低了该蛋白质的弹性和热稳定性。为了揭示SH1螺旋参与依赖于ATP的运动域的构象变化，我们利用基于GFP的荧光共振能量转移方法研究了R689H突变对转化器构象变化的影响。虽然突变似乎并不强烈地影响构象，但我们发现它显著降低了ATP诱导的与恢复期相对应的构象转变所需的激活能。鉴于突变对肌球蛋白力学性质的影响，我们认为SH1螺旋在肌球蛋白运动域构象变化的机械力化学能量转换中起着重要作用。
The SH1 helix is a joint that links the converter subdomain to the rest of the myosin motor domain. Recently, we showed that a mutation within the SH1 helix in Dictyostelium myosin II (R689H) reduced the elasticity and thermal stability of the protein. To reveal the involvement of the SH1 helix in ATP-dependent conformational changes of the motor domain, we have investigated the effects of the R689H mutation on the conformational changes of the converter, using a GFP-based fluorescence resonance energy transfer method. Although the mutation does not seem to strongly affect conformations, we found that it significantly reduced the activation energy required for the ATP-induced conformational transition corresponding to the recovery stroke. Given the effects of the mutation on the mechanical properties of myosin, we propose that the SH1 helix plays an important role in the mechanochemical energy conversion underlying the conformational change of the myosin motor domain.
影响因子：
2.9
作者：
BEECE, D;EISENSTEIN, L;YUE, KT
通讯作者：
YUE, KT
盘基网柄菌肌球蛋白截头的镁 (II)-焦磷酸复合物的 X 射线结构，分辨率为 2.7 A。
影响因子：
2.9
作者：
Smith,CA;Rayment,I
通讯作者：
Rayment,I