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相关概念视频

ATP Synthase: Structure01:18

ATP Synthase: Structure

16.2K
ATP synthase or ATPase is among the most conserved proteins found in bacteria, mammals, and plants. This enzyme can catalyze a forward reaction in response to the electrochemical gradient, producing ATP from ADP and inorganic phosphate. ATP synthase can also work in a reverse direction by hydrolyzing ATP and generating an electrochemical gradient. Different forms of ATP synthases have evolved special features to meet the specific demands of the cell. Based on their specific feature, ATP...
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Cryo-electron Microscopy01:28

Cryo-electron Microscopy

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Conventional electron microscopy (EM) involves dehydration, fixation, and staining of biological samples, which distorts the native state of biological molecules and results in several artifacts. Also, the high-energy electron beam damages the sample and makes it difficult to obtain high-resolution images. These issues can be addressed using cryo-EM, which uses frozen samples and gentler electron beams. The technique was developed by Jacques Dubochet, Joachim Frank, and Richard Henderson, for...
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Electron Microscope Tomography and Single-particle Reconstruction01:07

Electron Microscope Tomography and Single-particle Reconstruction

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Transmission electron microscopy (TEM) can be used to determine the 3D structure of biological samples with the help of techniques such as electron microscope tomography and single-particle reconstruction. While single-particle reconstruction can examine macromolecules and macromolecular complexes in vitro conditions only, tomography permits the study of cell components or small cells in vivo.
Electron Tomography
Electron tomography can be performed either in TEM or STEM (scanning transmission...
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相关实验视频

Updated: May 3, 2026

Visualization of ATP Synthase Dimers in Mitochondria by Electron Cryo-tomography
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通过冷电子显微镜捕获的GroEL的ATP结合状态.

N A Ranson1, G W Farr, A M Roseman

  • 1Department of Crystallography, Birkbeck College London, Malet Street, London WC1E 7HX, United Kingdom. n.ranson@bbk.ac.uk

Cell
|January 10, 2002
PubMed
概括
此摘要是机器生成的。

沙佩罗宁GroEL蛋白折叠周期涉及合作性ATP结合,激活一个环折叠,而另一个环释放基质. 结构洞察力揭示了域移动和盐桥变化,这些变化对这个过程和分子机器合作性至关重要.

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相关实验视频

Last Updated: May 3, 2026

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Visualization of ATP Synthase Dimers in Mitochondria by Electron Cryo-tomography

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科学领域:

  • 生物化学 生物化学
  • 结构生物学 结构生物学
  • 分子机器分子机器

背景情况:

  • 沙佩罗宁GroEL通过一种循环过程促进蛋白质折叠,其中包括ATP结合和水解.
  • GroEL 作为一个双环复合体运作,每个环能够结合ATP和基质.
  • 了解GroEL的合作功能机制是理解蛋白质平衡的关键.

研究的目的:

  • 为了阐明护卫者GroEL的蛋白质折叠周期的结构基础.
  • 调查ATP结合在GroEL的结构变化和合作性中的作用.
  • 开发解释ATP诱导的基质释放和环间合作性的结构模型.

主要方法:

  • 低温电子显微镜 (cryo-EM) 用于确定GroEL-ATP复合物的结构.
  • 原子结构与冷电磁密度图相匹配.
  • 对与GroEL和GroEL-GroES-ADP复合体结合的ATP结构变化的分析.

主要成果:

  • GroEL-ATP结构显示了中间域的向下旋转.
  • 观察到从基质切换到ATP结合域的跨子单元盐桥接触.
  • 结构数据表明在ATP结合时降低多亲和力和合作性的模型.

结论:

  • 这项研究为GroEL.中ATP诱导的形状变化提供了一个结构机制.
  • 建议GroEL的合作模式,包括盐桥切换.
  • 这些发现为其他环形分子机器的合作提供了洞察力.