• 主题
高级搜索  >
历史搜索 清空历史
首页> 外文期刊>Journal of Molecular Biology >Structure of the Entire Stalk Region of the Dynein Motor Domain
【24h】

Structure of the Entire Stalk Region of the Dynein Motor Domain

机译：Dynein电机域的整个茎区域的结构

获取原文
获取原文并翻译 | 示例
           
页面导航
  • 摘要
  • 著录项
  • 相似文献
  • 相关主题

摘要

Dyneins are large microtubule-based motor complexes that power a range of cellular processes including the transport of organelles, as well as the beating of cilia and flagella. The motor domain is located within the dynein heavy chain and comprises an N-terminal mechanical linker element, a central ring of six AAA+ modules of which four bind or hydrolyze ATP, and a long stalk extending from the AAA+ ring with a microtubule-binding domain (MTBD) at its tip. A crucial mechanism underlying the motile activity of cytoskeletal motor proteins is precise coupling between the ATPase and track-binding activities. In dynein, a stalk region consisting of a long (~ 15 nm) antiparallel coiled coil separates these two activities, which must facilitate communication between them. This communication is mediated by a small degree of helix sliding in the coiled coil. However, no high-resolution structure is available of the entire stalk region including the MTBD. Here, we have reported the structure of the entire stalk region of mouse cytoplasmic dynein in a weak microtubule-binding state, which was determined using X-ray crystallography, and have compared it with the dynein motor domain from Dictyostelium discoideum in a strong microtubule-binding state and with a mouse MTBD with its distal portion of the coiled coil fused to seryl-tRNA synthetase from Thermus thermophilus. Our results strongly support the helix-sliding model based on the complete structure of the dynein stalk with a different form of coiled-coil packing. We also propose a plausible mechanism of helix sliding together with further analysis using molecular dynamics simulations. Our results present the importance of conserved praline residues for an elastic motion of stalk coiled coil and imply the manner of change between high-affinity state and low-affinity state of MTBD.
机译：动力蛋白是基于微管的大型运动复合物，可驱动一系列细胞过程，包括细胞器的运输以及纤毛和鞭毛的跳动。马达域位于动力蛋白重链内，包括一个N末端机械连接子元件，一个由六个AAA +模块组成的中心环，其中四个与ATP结合或水解，以及一个长柄，该长柄从AAA +环延伸出来并带有微管结合域。 （MTBD）。细胞骨架运动蛋白运动活性的潜在关键机制是ATPase和轨道结合活性之间的精确偶联。在动力蛋白中，由长（〜15 nm）反平行螺旋线圈组成的茎区域将这两个活动分开，这必须促进它们之间的通信。这种通信是由螺旋线圈中的少量螺旋滑动所介导的。但是，包括MTBD在内的整个茎区域都没有高分辨率结构。在这里，我们报道了使用X射线晶体学测定的弱微管结合状态下小鼠细胞质动力蛋白的整个茎区域的结构，并将其与来自盘基网柄菌的动力蛋白域在强力微管中进行了比较。小鼠MTBD的结合状态，其卷曲螺旋的远端部分与嗜热栖热菌的Seryl-tRNA合成酶融合。我们的结果有力地支持了基于动力蛋白茎完整结构的螺旋滑动模型，并具有不同形式的盘绕盘根。我们还提出了一种合理的螺旋滑动机理，并使用分子动力学模拟进行了进一步分析。我们的结果表明保守的果仁糖残留物对茎秆盘绕线圈的弹性运动的重要性，并暗示了MTBD在高亲和力状态和低亲和力状态之间变化的方式。

著录项

相似文献

  • 外文文献
  • 中文文献
  • 专利
获取原文

客服邮箱：kefu@zhangqiaokeyan.com

京公网安备：11010802029741号 ICP备案号：京ICP备15016152号-6 六维联合信息科技 (北京) 有限公司©版权所有

  • 客服微信

  • 服务号