• 主题
高级搜索  >
历史搜索 清空历史
首页> 外文期刊>Journal of Molecular Biology >Three-dimensional structure of the M-region (bare zone) of vertebrate striated muscle myosin filaments by single-particle analysis.
【24h】

Three-dimensional structure of the M-region (bare zone) of vertebrate striated muscle myosin filaments by single-particle analysis.

机译：脊椎动物横纹肌肌球蛋白丝的M区（裸露区）的三维结构，通过单颗粒分析。

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

The rods of anti-parallel myosin molecules overlap at the centre of bipolar myosin filaments to produce an M-region (bare zone) that is free of myosin heads. Beyond the M-region edges, myosin molecules aggregate in a parallel fashion to yield the bridge regions of the myosin filaments. Adjacent myosin filaments in striated muscle A-bands are cross-linked by the M-band. Vertebrate striated muscle myosin filaments have a 3-fold rotational symmetry around their long axes. In addition, at the centre of the M-region, there are three 2-fold axes perpendicular to the filament long axis, giving the whole filament dihedral 32-point group symmetry. Here we describe the three-dimensional structure obtained by a single-particle analysis of the M-region of myosin filaments from goldfish skeletal muscle under relaxing conditions and as viewed in negative stain. This is the first single-particle reconstruction of isolated M-regions. The resulting three-dimensional reconstruction reveals details to about 55 A resolution of the density distribution in the five main nonmyosin densities in the M-band (M6', M4', M1, M4 and M6) and in the myosin head crowns (P1, P2 and P3) at the M-region edges. The outermost crowns in the reconstruction were identified specifically by their close similarity to the corresponding crown levels in our previously published bridge region reconstructions. The packing of myosin molecules into the M-region structure is discussed, and some unidentified densities are highlighted.
机译：反平行肌球蛋白分子的棒在双极肌球蛋白丝的中心重叠，产生一个没有肌球蛋白头部的M区（裸区）。除了M区边缘，肌球蛋白分子以平行方式聚集，以产生肌球蛋白丝的桥区。横纹肌A波段中相邻的肌球蛋白丝通过M波段交联。脊椎动物的横纹肌肌球蛋白丝围绕其长轴具有3倍的旋转对称性。此外，在M区域的中心，有三个垂直于灯丝长轴的2倍轴，使整个灯丝二面体32点群对称。在这里，我们描述了通过在放松条件下以及在负染下观察到的金鱼骨骼肌肌球蛋白丝M区的单颗粒分析获得的三维结构。这是孤立的M区域的第一个单粒子重建。进行的三维重建显示了M波段（M6'，M4'，M1，M4和M6）和肌球蛋白头冠（P1， P2和P3）在M区边缘。重建中最外面的冠是通过与我们先前发布的桥梁区域重建中的相应冠水平紧密相似而专门确定的。讨论了肌球蛋白分子在M区结构中的堆积，并突出了一些不确定的密度。

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