亚纳贝纳菌体A-1的完整尾部机器的结构 (L)
Rong-Cheng Yu1,2, Feng Yang1,3, Hong-Yan Zhang1,2
1School of Life Sciences, Division of Life Sciences and Medicine, University of Science and Technology of China, Hefei, China.
Nature communications
|March 27, 2024
概括
使用冷EM解决了Myoviridae蓝虫A-1(L) 尾部机器结构. 这揭示了它的组成部分和功能,有助于其在合成生物学中的应用.
科学领域:
- 结构生物学是结构生物学.
- 病毒学 病毒学
- 微生物学 微生物学
背景情况:
- 蓝菌是感染蓝菌的病毒,在水生生态系统中起着至关重要的作用.
- 菌类家族Myoviridae,包括虫A-1(L),具有复杂的收缩尾巴,对感染至关重要.
- 了解菌体结构是利用它们用于生物技术应用的关键.
研究的目的:
- 为了确定高分辨率冷电子显微镜 (cryo-EM) 结构的完整尾部机器的食动物A-1(L).
- 阐明部,收缩尾部和基板的结构组织,包括相关纤维.
- 确定参与宿主受体结合和水解活性的功能域.
主要方法:
- 高分辨率冷电子显微镜 (cryo-EM) 用于结构确定.
- 生物化学测试用于研究蛋白质功能和相互作用.
- 用于基因组重新注释的生物信息分析.
主要成果:
- 完好无损的尾部机器结构揭示了一个十二角形门户,一个独特的五角形部结构,带有珠子链状的纤维,以及长达1045的收缩尾部.
- 尾部包括测量带,管和膜蛋白,以五个组成部分的基板结束.
- 结构和生物化学数据确定了基板枢纽和两个宿主受体结合域在尾纤维中的双重水解活性.
- 根据结构发现,A-1 (L) 基因组进行了重新注释.
结论:
- 蓝A-1(L) 尾机的详细结构为其感染机制提供了前所未有的洞察力.
- 已识别的功能域为工程食菌与宿主相互作用提供了目标.
- 这些发现支持A-1(L) 作为合成生物学应用的底盘蓝体的潜力.
相关概念视频
01:24Microtubules in Cell Motility
3.3K
Microtubules are thick hollow cylindrical proteins that help form the cytoskeleton. Microtubules have varied roles in the cell. These filaments help form cellular appendages like cilia and flagella, which are responsible for locomotion. The cilia arise from basal bodies, separated from the main body by a membrane-like structure forming the transition zone. This zone is the gate for the entry of lipids and proteins, creating a unique composition of lipids and proteins in the ciliary membrane and...
3.3K
01:15Overview of Myosin Structure and Function
4.3K
Myosins are a family of molecular motor proteins, first identified in the skeletal muscles, where they are responsible for muscle contraction. Along with their role in muscle contraction, these proteins also play a role in the intracellular transport of molecules and vesicles. There are twenty-four classes of myosins based on their domain sequence and organization. Of the twenty-four, six classes (Myosin I, Myosin II, Myosin V, Myosin VI, Myosin VII, and Myosin X) have been well...
4.3K
01:48ATP Synthase: Mechanism
14.6K
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...
14.6K
01:18ATP Synthase: Structure
12.3K
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...
12.3K
01:30ATP Driven Pumps III: V-type Pumps
3.7K
V-type pumps are ATP-driven pumps found in the vacuolar membranes of plants, yeast, endosomal and lysosomal membranes of animal cells, plasma membranes of a few specialized eukaryotic cells, and some prokaryotes. They are also known as the V1Vo-ATPase, that couple ATP hydrolysis to transport protons against a concentration gradient.
The peripheral or cytosolic V1 domain with eight subunits is involved in ATP hydrolysis. The integral or transmembrane V0 domain containing at least five subunits...
The peripheral or cytosolic V1 domain with eight subunits is involved in ATP hydrolysis. The integral or transmembrane V0 domain containing at least five subunits...
3.7K
01:45Tail-anchoring of Proteins in the ER Membrane
3.1K
Tail-anchored, or TA, proteins are estimated to make up to 3-5% of membrane proteins found in the eukaryotic cell. Such proteins have a single transmembrane domain located approximately 30 amino acid residues upstream from the C-terminal end. As a result, the signal recognition particle (SRP) cannot guide a TA protein to the ER membrane for cotranslational insertion. Hence, they are integrated into the ER membrane post-translationally using their C-terminal end as the anchor. TA proteins...
3.1K