Jove
Visualize
联系我们
JoVE
x logofacebook logolinkedin logoyoutube logo
关于 JoVE
概览领导团队博客JoVE 帮助中心
作者
出版流程编辑委员会范围与政策同行评审常见问题投稿
图书馆员
用户评价订阅访问资源图书馆顾问委员会常见问题
研究
JoVE JournalMethods CollectionsJoVE Encyclopedia of Experiments存档
教育
JoVE CoreJoVE BusinessJoVE Science EducationJoVE Lab Manual教师资源中心教师网站
使用条款与条件
隐私政策
政策

相关概念视频

Protein Complexes with Interchangeable Parts01:57

Protein Complexes with Interchangeable Parts

2.1K
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...
2.1K
Protein Complexes with Interchangeable Parts01:57

Protein Complexes with Interchangeable Parts

1.0K
1.0K
ATP Synthase: Structure01:18

ATP Synthase: Structure

16.1K
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...
16.1K
Protein Complex Assembly02:41

Protein Complex Assembly

12.5K
Proteins can form homomeric complexes with another unit of the same protein or heteromeric complexes with different types.  Most protein complexes self-assemble spontaneously via ordered pathways, while some proteins need assembly factors that guide their proper assembly. Despite the crowded intracellular environment, proteins usually interact with their correct partners and form functional complexes.
Many viruses self-assemble into a fully functional unit using the infected host cell to...
12.5K
Protein Complex Assembly02:41

Protein Complex Assembly

1.6K
1.6K
Peptidoglycan Synthesis01:28

Peptidoglycan Synthesis

4.7K
Structure of PeptidoglycanPeptidoglycan is a vital structural component of the bacterial cell wall, providing mechanical strength and shape to the cell. It consists of repeating units of two sugars—N-acetylglucosamine (NAG) and N-acetylmuramic acid (NAM)—linked by β-1,4 glycosidic bonds. These sugar chains are cross-linked by short peptide chains, forming a mesh-like polymer that surrounds the bacterial plasma membrane.Cytoplasmic Phase – Precursor SynthesisPeptidoglycan...
4.7K

您也可能阅读

相关文章

通过共同作者、期刊和引用图与本文相关的文章。

排序
Same author

Library Docking for Cannabinoid-2 Receptor Ligands.

Journal of medicinal chemistry·2026
Same author

Author Correction: Synthesis of enantioenriched atropisomers by biocatalytic deracemization.

Nature·2026
Same author

Large-scale discovery platform enables identification of peptides targeting drug-resistant candidiasis.

Cell reports methods·2026
Same author

Chemoselective Halogenation of Premarineosin A for Next-Generation Antimalarial Development.

bioRxiv : the preprint server for biology·2026
Same author

High-Throughput Screening of Isomeric Reaction Products by Droplet Microfluidics Coupled to Cyclic Ion Mobility-Mass Spectrometry.

Analytical chemistry·2026
Same author

Author Correction: A µ-opioid receptor superagonist analgesic with minimal adverse effects.

Nature·2026

相关实验视频

Updated: Apr 27, 2026

From a Natural Product to Its Biosynthetic Gene Cluster: A Demonstration Using Polyketomycin from Streptomyces diastatochromogenes Tü6028
09:08

From a Natural Product to Its Biosynthetic Gene Cluster: A Demonstration Using Polyketomycin from Streptomyces diastatochromogenes Tü6028

Published on: January 13, 2017

18.4K

一个模块化多基化合成酶的结构.

Somnath Dutta1, Jonathan R Whicher2, Douglas A Hansen3

  • 11] Life Sciences Institute, University of Michigan, Ann Arbor, Michigan 48109, USA [2].

Nature
|June 27, 2014
PubMed
概括
此摘要是机器生成的。

研究人员研究了I型多基酸合成酶 (PKSs),揭示了基底转移的新型结构. 这一发现为这些关键的生物合成酶的分子机制提供了新的见解.

更多相关视频

The Logic, Experimental Steps, and Potential of Heterologous Natural Product Biosynthesis Featuring the Complex Antibiotic Erythromycin A Produced Through E. coli
10:41

The Logic, Experimental Steps, and Potential of Heterologous Natural Product Biosynthesis Featuring the Complex Antibiotic Erythromycin A Produced Through E. coli

Published on: January 13, 2013

18.0K
X-Ray Crystallography to Study the Oligomeric State Transition of the Thermotoga maritima M42 Aminopeptidase TmPep1050
11:27

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

Published on: May 13, 2020

3.4K

相关实验视频

Last Updated: Apr 27, 2026

From a Natural Product to Its Biosynthetic Gene Cluster: A Demonstration Using Polyketomycin from Streptomyces diastatochromogenes Tü6028
09:08

From a Natural Product to Its Biosynthetic Gene Cluster: A Demonstration Using Polyketomycin from Streptomyces diastatochromogenes Tü6028

Published on: January 13, 2017

18.4K
The Logic, Experimental Steps, and Potential of Heterologous Natural Product Biosynthesis Featuring the Complex Antibiotic Erythromycin A Produced Through E. coli
10:41

The Logic, Experimental Steps, and Potential of Heterologous Natural Product Biosynthesis Featuring the Complex Antibiotic Erythromycin A Produced Through E. coli

Published on: January 13, 2013

18.0K
X-Ray Crystallography to Study the Oligomeric State Transition of the Thermotoga maritima M42 Aminopeptidase TmPep1050
11:27

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

Published on: May 13, 2020

3.4K

科学领域:

  • 生物化学 生物化学
  • 分子生物学分子生物学
  • 结构生物学 结构生物学

背景情况:

  • 聚基化物天然产品具有多样化的结构和生物活性.
  • I型多基合成酶 (PKSs) 是大型模块化酶,负责它们的生物合成.
  • 了解PKS架构是阐明聚基合成途径的关键.

研究的目的:

  • 确定来自Streptomyces venezuelae*的全长PKS模块的三维结构.
  • 阐明PKS模块内和之间基质转移的机制.
  • 建立PKS系统结构分析的新模型.

主要方法:

  • 使用电子冷显微镜 (cryo-EM) 来获取高分辨率的结构数据.
  • 产生了以亚纳米分辨率的三维重建.
  • 与同类酶进行结构比较,例如哺乳动物脂肪酸合成酶.

主要成果:

  • 发现了一种独特的PKS模块架构,与哺乳动物脂肪酸合成酶不同.
  • 一个单一的反应室可以容纳内部模块载体域.
  • 独立的入口点促进了模块间基板的交付,与模块内处理不同.

结论:

  • 这项研究提供了第一个结构证据,证明了PKS中内和间基质的转移.
  • 提出了PKS酶功能和基质通道的新型模型.
  • 这项工作使复杂PKS机械的分子解剖的新策略成为可能.