Domain motions of EF-G bound to the 70S ribosome: insights from a hand-shaking between multi-resolution structures.
Domain motions of EF-G bound to the 70S ribosome: insights from a hand-shaking between multi-resolution structures.
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DOI：
10.1016/s0006-3495(00)76416-2
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发表时间：
2000-09
影响因子：
3.4
通讯作者：
W. Wriggers;W. Wriggers;R. Agrawal;R. Agrawal;D. Drew;Andrew McCammon;J. Frank;J. Frank
中科院分区：
文献类型：
--
作者：
W. Wriggers;W. Wriggers;R. Agrawal;R. Agrawal;D. Drew;Andrew McCammon;J. Frank;J. Frank
结合分子建模和信息处理技术，根据冷冻电子显微镜 (cryo-EM) 数据，细化核糖体结合形式的转位酶 (EF-G) 的结构。我们设计了一种基于矢量量化和力场方法的新型多尺度细化方法，该方法在 GDP·EF-G 的灵活对接结构与 17Å 分辨率的冷冻电镜密度图之间提供了良好的一致性。这一改进揭示了 70S 核糖体上显着的“诱导契合”构象变化，主要涉及 EF-G 的结构域 III、IV 和 V。EF-G 结构保留区域的重排在柔性接头的介导和引导下，定义了与核糖体 GTP 酶相关中心相互作用的位点。
Molecular modeling and information processing techniques were combined to refine the structure of translocase (EF-G) in the ribosome-bound form against data from cryoelectron microscopy (cryo-EM). We devised a novel multi-scale refinement method based on vector quantization and force-field methods that gives excellent agreement between the flexibly docked structure of GDP · EF-G and the cryo-EM density map at 17Å resolution. The refinement reveals a dramatic "induced fit" conformational change on the 70S ribosome, mainly involving EF-G's domains III, IV, and V. The rearrangement of EF-G's structurally preserved regions, mediated and guided by flexible linkers, defines the site of interaction with the GTPase-associated center of the ribosome.