热 (Chaetomium thermophilum) TOM复合物的结构与结合的前蛋白质有关
Ahmed-Noor A Agip1, Pamela Ornelas1, Tzu-Jing Yang2
1Department of Structural Biology, Max Planck Institute of Biophysics, Frankfurt 60438, Germany.
概括
线粒体通过TOM复合体进口蛋白质. 新的结构揭示了Tom20受体的新结构.
科学领域:
- 线粒体生物学 线粒体生物学
- 蛋白质转位的转位是蛋白质转位.
- 结构生物学是结构生物学.
背景情况:
- 线粒体通过TOM复合体从细胞质中进口蛋白质.
- 该TOM复合物促进蛋白质在外层线粒体膜的转移.
研究的目的:
- 阐明TOM复合体的结构和动态机制.
- 了解蛋白质进口到线粒体的早期阶段.
主要方法:
- 单粒子电子冷显微镜 (cryo-EM) 是一种技术.
- 对TOM核心和全光复合体的结构分析.
- 蛋白质结合和自由状态的生物化学表征.
主要成果:
- 从*Chaetomium thermophilum**中确定了TOM核心和全光复合物的结构.
- 揭示了TOM全息复合体中两个Tom20受体子单元的对称排列.
- 观察了Tom20的动态构造,为蛋白前结合和转位启动提供了洞察力.
结论:
- 姆全息复合体表现出一个动态的姆20受体排列.
- 对前蛋白结合的Tom20的结构洞察力揭示了早期蛋白质转位事件.
- 这项研究为线粒体蛋白质进口机制提供了高分辨率的结构基础.
更多相关视频
10:01Combining Chemical Cross-linking and Mass Spectrometry of Intact Protein Complexes to Study the Architecture of Multi-subunit Protein Assemblies
Published on: November 28, 2017
19.8K
11:27X-Ray Crystallography to Study the Oligomeric State Transition of the Thermotoga maritima M42 Aminopeptidase TmPep1050
Published on: May 13, 2020
4.0K
相关概念视频
Protein Complex Assembly
10.9K
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...
Many viruses self-assemble into a fully functional unit using the infected host cell to...
10.9K
Molecular Chaperones and Protein Folding
18.5K
The native conformation of a protein is formed by interactions between the side chains of its constituent amino acids. When the amino acids cannot form these interactions, the protein cannot fold by itself and needs chaperones. Notably, chaperones do not relay any additional information required for the folding of polypeptides; the native conformation of a protein is determined solely by its amino acid sequence. Chaperones catalyze protein folding without being a part of the folded protein.
The...
The...
18.5K
Protein Transport to the Stroma
1.9K
Chloroplasts are triple membrane structures with an outer membrane, an inner membrane, and a thylakoid membrane, each containing distinct metabolite transporters, membrane translocons, and enzymes. Appropriate sorting and translocating these proteins to their correct membrane systems is essential for chloroplast function.
Protein complexes called the translocon of the outer chloroplast membrane or TOC complex, and the translocon of the inner chloroplast membrane or TIC complex mediate the...
Protein complexes called the translocon of the outer chloroplast membrane or TOC complex, and the translocon of the inner chloroplast membrane or TIC complex mediate the...
1.9K
Structure of Cadherins
3.6K
The cadherins were one of the first cell adhesion molecules discovered; the term “cadherins” is based on their calcium-dependent adhering properties. The first cadherins discovered on the epithelial, neuronal, and placental cells were named E-cadherin, P-cadherin, and N-cadherin, respectively. These classical cadherins share sequence and structural similarities. Other cadherins, including those involved in cell signaling, are grouped into non-classical cadherins. This...
3.6K
Protein Folding
121.5K
Overview
121.5K
Protein Organization
7.2K
Proteins are polymers of amino acid residues. They are versatile and responsible for different cellular functions, including DNA replication, molecular transport, catalysis, and structural support. Proteins have a hierarchical structure comprising at least three levels of organization: primary, secondary, and tertiary structure. Some large proteins have a quaternary structure where individual protein subunits are linked together.
The primary structure of a protein is its amino acid sequence....
The primary structure of a protein is its amino acid sequence....
7.2K
