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相关概念视频

ATP Synthase: Structure01:18

ATP Synthase: Structure

17.7K
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...
17.7K
Molecular Models02:00

Molecular Models

45.5K
Physical models representing molecular architectures of chemical compounds play essential roles in understanding chemistry. The use of molecular models makes it easier to visualize the structures and shapes of atoms and molecules.
45.5K
Structures of Carboxylic Acid Derivatives01:28

Structures of Carboxylic Acid Derivatives

4.1K
Structure of Carboxylic Acid Derivatives
Carboxylic acid derivatives contain an acyl group attached to a heteroatom such as chlorine, oxygen, or nitrogen. The carbonyl carbon and oxygen are both sp2-hybridized with an unhybridized p orbital.
The three sp2 orbitals of the carbonyl carbon form three σ bonds, one each with the carbonyl oxygen, the α carbon, and the heteroatom, whereas the other two sp2 orbitals of the carbonyl oxygen are occupied by the lone pairs. Further, the unhybridized p...
4.1K
ATP Synthase: Mechanism01:48

ATP Synthase: Mechanism

18.8K
In animals, the mitochondrial F1F0 ATP synthase is the key protein that synthesizes ATP molecules through a complex catalytic mechanism. While the nuclear genome encodes the majority of ATP synthase subunits, the mitochondrial genome encodes some of the enzyme's most critical components. The formation of this multi-subunit enzyme is a complex multi-step process regulated at the level of transcription, translation, and assembly. Defects in one or more of these steps can result in decreased...
18.8K
Protein Complexes with Interchangeable Parts01:57

Protein Complexes with Interchangeable Parts

3.1K
Groups of proteins may form a complex where each protein in this complex has a different role in the overall execution of the complex’s function. Often some of the proteins in the complex can be replaced by a closely related variant to give a complex that contains many of the same components yet is functionally distinct.
The SCF ubiquitin ligase is a protein complex of five individual proteins. This complex attaches ubiquitin to other target proteins to mark them for degradation. In order...
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Protein Complexes with Interchangeable Parts01:57

Protein Complexes with Interchangeable Parts

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相关实验视频

Updated: Apr 1, 2026

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

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500kDa酵母乙-CoA碳酸酶全酶二元体的晶体结构

Jia Wei1, Liang Tong1

  • 1Department of Biological Sciences, Columbia University, New York, New York 10027, USA.

Nature
|October 13, 2015
PubMed
概括

在Saccharomyces cerevisiae的晶体结构中,可以发现其独特的结构和催化机制. 这一发现为脂肪酸代谢和糖尿病和癌症等疾病的潜在药物标提供了洞察力.

科学领域:

  • 生物化学
  • 结构生物学
  • 酵素学

背景情况:

  • 乙-CoA碳酸酶 (ACC) 对脂肪酸代谢至关重要,也是治疗糖尿病和癌症的点.
  • 糖菌 (Saccharomyces cerevisiae ACC) 在非常长链脂肪酸生产和核膜维护中起着关键作用.
  • 虽然ACC和其他生物依碳酶的结构已知,但全酶结构仍然难以捉摸.

研究的目的:

  • 为了确定Saccharomyces cerevisiae全长乙-CoA碳酶 (ScACC) 全酶二聚体的晶体结构.
  • 阐明SCACC独特的催化机制和调节的结构基础.
  • 了解针对ACC的药物发现的结构性影响.

主要方法:

  • 射线晶体学
  • 对ScACC的500kDa全酶二元结构的分析
  • 与个别域和相关酶的结构进行比较

主要成果:

  • 确定了500kDa的ScACC全酶二聚体的晶体结构,揭示了与其他依赖生物的碳酸酶不同的独特结构.
  • 中部区域包含五个域,对于定位生物碳酸酶 (BC) 和碳酸转移酶 (CT) 催化域至关重要.
  • 在全酶中,BC域作为二聚体存在,与其单聚体形式分离不同,单独解释其催化不活性并揭示抑制机制.

更多相关视频

Combining X-Ray Crystallography with Small Angle X-Ray Scattering to Model Unstructured Regions of Nsa1 from S. Cerevisiae
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Combining X-Ray Crystallography with Small Angle X-Ray Scattering to Model Unstructured Regions of Nsa1 from S. Cerevisiae

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X-Ray Crystallography to Study the Oligomeric State Transition of the Thermotoga maritima M42 Aminopeptidase TmPep1050
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X-Ray Crystallography to Study the Oligomeric State Transition of the Thermotoga maritima M42 Aminopeptidase TmPep1050

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相关实验视频

Last Updated: Apr 1, 2026

Visualization of ATP Synthase Dimers in Mitochondria by Electron Cryo-tomography
10:39

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

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Combining X-Ray Crystallography with Small Angle X-Ray Scattering to Model Unstructured Regions of Nsa1 from S. Cerevisiae
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Combining X-Ray Crystallography with Small Angle X-Ray Scattering to Model Unstructured Regions of Nsa1 from S. Cerevisiae

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X-Ray Crystallography to Study the Oligomeric State Transition of the Thermotoga maritima M42 Aminopeptidase TmPep1050
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X-Ray Crystallography to Study the Oligomeric State Transition of the Thermotoga maritima M42 Aminopeptidase TmPep1050

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结论:

  • 确定的ScACC全酶结构为真核细胞的ACC功能提供了前所未有的洞察力.
  • 结构发现解释了单独的BC域的催化不活性,并阐明了由索拉A和酸化抑制ACC的机制.
  • 这项工作为针对各种疾病的结构性药物设计奠定了基础.