Institute for Protein Research, Osaka University, Osaka, Japan. Department of Macromolecular Science, Graduate School of Science, Osaka University, Osaka, Japan.
Nat Struct Mol Biol. 2011 Jun;18(6):638-42. doi: 10.1038/nsmb.2074. Epub 2011 May 22.
Dyneins are large microtubule-based motors that power a wide variety of cellular processes. Here we report a 4.5-Å 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.
动力蛋白是一种基于微管的大型分子马达，能够为多种细胞过程提供动力。在此，我们报道了来自盘基网柄菌的细胞质动力蛋白完整功能马达域与 ADP 的 4.5Å X 射线晶体结构分析，揭示了马达活性所需的功能单元的详细结构，包括 ATP 水解环、长卷曲螺旋微管结合臂和产生力的杆状连接臂。我们发现了一个由两个长卷曲螺旋组成的 Y 形突起——臂和新鉴定的“支柱”。该结构支持我们的模型，即支柱卷曲螺旋积极促进环中的主要 ATP 酶位点与臂卷曲螺旋末端的微管结合位点之间的通讯。我们的工作还深入了解了两个马达域如何在细胞质动力蛋白的功能二聚体形式中相互排列和相互作用。
