首页> 外文期刊>Nature >A 35-ANGSTROM MOVEMENT OF SMOOTH MUSCLE MYOSIN ON ADP RELEASE
【24h】

A 35-ANGSTROM MOVEMENT OF SMOOTH MUSCLE MYOSIN ON ADP RELEASE

机译:ADP释放上35肌平滑肌肌球蛋白的运动

获取原文
获取原文并翻译 | 示例
           

摘要

MYOSIN II crossbridges interact with F-actin producing power-strokes of around 100 Angstrom (refs 1, 2), during which the products of ATP hydrolysis are released(3,5). This has been postulated to involve an articulation of the myosin head (S1) on actin, or substantial conformational changes in S1 itself(6-8). Small movements of the regulatory light chain have been detected (see, for example, refs 9, 10), but most data suggest that the bulk of S1 does not move on actin during crossbridge cyclings(8,11). Here we present three-dimensional maps of S1-decorated F-actin in the presence and absence of MgADP. The myosin motor domain is similar in both states but there are major orientational differences in the chain-binding domain, This domain acts as a rigid level arm pivoting about the end of the motor domain and swinging similar to 23 degrees, resulting in a similar to 35-Angstrom step. Small, nucleotide-mediated conformational changes in the motor domain(14-16) may thus be converted by the light-chain domain into large movement steps.
机译:MYOSIN II跨桥与F-肌动蛋白相互作用,产生约100埃的动力冲程(参考文献1、2),在此期间释放ATP水解的产物(3,5)。据推测,这涉及肌动蛋白上肌球蛋白头(S1)的铰接,或S1本身的构象变化很大(6-8)。已检测到调节性轻链的微小运动(例如,参见参考文献9、10),但是大多数数据表明,大部分S1在跨桥循环中不会在肌动蛋白上运动(8,11)。在这里,我们介绍存在和不存在MgADP的S1装饰的F-肌动蛋白的三维图。肌球蛋白的运动域在两种状态下都相似,但是在链结合域中存在主要的方向差异。该域充当刚性水平臂,围绕运动域的末端枢转并摆动类似23度,从而导致35埃步。运动域(14-16)中核苷酸介导的小构象变化可能会被轻链结构域转换成较大的运动步伐。

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