X-ray structure of a functional full-length dynein motor domain
X-ray structure of a functional full-length dynein motor domain
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DOI：
10.1038/nsmb.2074
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发表时间：
2011-06-01
影响因子：
16.8
通讯作者：
Kurisu, Genji
中科院分区：
文献类型：
--
作者：
Kon, Takahide;Sutoh, Kazuo;Kurisu, Genji
动力蛋白是以微管为基础的大型马达，为各种各样的细胞过程提供动力。在这里，我们报告了一个4.5埃的X射线结晶学分析的细胞质动力蛋白与ADP的整个功能运动结构域，揭示了运动活动所需的功能单元的详细结构，包括ATP水解环，长盘绕微管结合柄和产生力量的棒状连接子。我们发现了一个由两个长卷曲组成的Y形突起--茎和新发现的“支柱”。这种结构支持我们的模型，在该模型中，支撑盘绕线圈积极地促进环中主要ATPase位点和茎盘绕线圈顶端的微管结合位点之间的通信。我们的工作还提供了对这两个运动域是如何排列的，以及它们如何在细胞质动力蛋白的功能二聚体形式中相互作用的见解。
Dyneins are large microtubule-based motors that power a wide variety of cellular processes. Here we report a 4.5-angstrom X-ray crystallographic analysis of the entire functional motor domain of cytoplasmic dynein with ADP from Dictyostelium discoideum, which has revealed the detailed architecture of the functional units required for motor activity, including the ATP-hydrolyzing ring, the long coiled-coil microtubule-binding stalk and the force-generating rod-like linker. We discovered a Y-shaped protrusion composed of two long coiled coils-the stalk and the newly identified 'strut'. This structure supports our model in which the strut coiled coil actively contributes to communication between the primary ATPase site in the ring and the microtubule-binding site at the tip of the stalk coiled coil. Our work also provides insight into how the two motor domains are arranged and how they interact with each other in a functional dimer form of cytoplasmic dynein.