ATP-induced transconformation of myosin revealed by determining three-dimensional positions of fluorophores from fluorescence energy transfer measurements.
ATP-induced transconformation of myosin revealed by determining three-dimensional positions of fluorophores from fluorescence energy transfer measurements.
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通过荧光能量转移测量确定荧光团的三维位置，揭示了 ATP 诱导的肌球蛋白转构。
DOI：
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发表时间：
2000
影响因子：
3
通讯作者：
T. Wakabayashi
中科院分区：
文献类型：
--
作者：
T. Yasunaga;Y. Suzuki;R. Ohkura;K. Sutoh;T. Wakabayashi
荧光共振能量转移法（FRET）是测量两个荧光团之间距离和检测生理条件下蛋白质结构变化的最重要技术之一。利用绿色荧光蛋白也是一项强有力的技术，已被用于阐明动态分子事件。从这些，我们已经开发了一种新的方法来确定荧光团的三维位置，通过结合FRET数据和其他结构信息。利用这种方法，我们可以测定atp诱导的截断盘基骨菌肌球蛋白在溶液中的三维结构变化。ADP水溶液中肌球蛋白的晶体结构与mgadpbefx结合的截断盘形骨肌球蛋白的晶体结构相似（I型结构），而ATP水溶液中肌球蛋白的晶体结构与mgadpvi结合的肌球蛋白的晶体结构相似（II型结构）。然而，在各种条件下，我们的任何FRET数据都无法解释mgadp结合的扇贝肌球蛋白的晶体结构（III型结构）。这表明III型晶体结构可能是一种瞬时的中间构象，无法用荧光能量转移检测到。
The method of fluorescence resonance energy transfer (FRET) is one of the most important techniques for measuring the distance between two fluorophores and for detecting the changes in protein structure under physiological conditions. The use of green fluorescent protein is also a powerful technology that has been used to elucidate dynamic molecular events. From these we have developed a novel method to determine the three-dimensional positions of fluorophores by combining the FRET data and other structural information available. Using this method, we could determine the ATP-induced changes of three-dimensional structure of truncated Dictyostelium myosin in solution. The myosin structure with ADP in solution was found to be similar to that of the crystal structure of MgADPBeFx-bound truncated Dictyostelium myosin (type I structure), whereas myosin with ATP in solution was similar to the crystal structure of MgAdPVi-bound one (type II structure). However, the crystal structure of MgADP-bound scallop myosin (type III structure) could not be explained by any of our FRET data under various conditions. This indicates that the type III crystal structure might represent a transient intermediate conformation that could not be detected using fluorescence energy transfer.
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影响因子：
3.4
作者：
Gordon, GW;Berry, G;Herman, B
通讯作者：
Herman, B
探索肌球蛋白中 SH1-SH2 螺旋的构象状态：一种交联方法。
影响因子：
2.9
作者：
Nitao,LK;Reisler,E
通讯作者：
Reisler,E
肌动球蛋白亚片段 1 复合物的结构：使用电子显微镜和 X 射线晶体学数据的搜索结果。
DOI：
10.1073/pnas.94.16.8533
发表时间：
1997
影响因子：
11.1
作者：
Mendelson,R;Morris,EP
通讯作者：
Morris,EP
影响因子：
2.9
作者：
Gulick, AM;Bauer, CB;Rayment, I
通讯作者：
Rayment, I
DOI：
10.1073/pnas.96.2.465
发表时间：
1999-01-19
影响因子：
11.1
作者：
Walker, M;Zhang, XZ;White, HD
通讯作者：
White, HD