图片提供了酸盐进口蛋白质的强大视角
David Speedman1, David B Sauer1
1Centre for Medicines Discovery, Nuffield Department of Medicine, University of Oxford, Oxford, UK.
Structure (London, England : 1993)
|July 12, 2024
概括
研究人员发现了酵母中的无机酸盐载体Pho90的新结合机制. 这些冷电子显微镜结构揭示了,基质和脂质如何与这种重要的蛋白相互作用.
科学领域:
- 结构生物学是结构生物学.
- 生物化学 生化学
- 分子生物学分子生物学
背景情况:
- 来自Saccharomyces cerevisiae的无机酸盐运输体Pho90是双重阳离子运输体家族的成员.
- 了解这些蛋白质的运输机制对于细胞酸盐平衡至关重要.
研究的目的:
- 为了确定无机酸盐输送器Pho90.0.的高分辨率结构.
- 阐明,基质和脂质与Pho90.0结合的机制.
主要方法:
- 使用冷电子显微镜 (cryo-EM) 来获得Pho90.的多重结构.
- 在获得的冷EM数据上进行了高分辨率的结构分析.
主要成果:
- Pho90的多个结构得到了显著的分辨率.
- 确定了,基质和脂质结合的新模式.
- 获得了对这种双重阳离子共传体家族成员的功能结构洞察.
结论:
- 确定的结构提供了对Pho90功能的详细分子理解.
- 这些发现提升了我们对Saccharomyces cerevisiae中酸盐运输的了解.
- 这项研究揭示了与更广泛的双重阳离子共导体家族相关的新型相互作用.
相关概念视频
Phosphorylation
50.2K
The addition or removal of phosphate groups from proteins is the most common chemical modification that regulates cellular processes. These modifications can affect the structure, activity, stability, and localization of proteins within cells as well as their interactions with other proteins.
During phosphorylation, protein kinases transfer the terminal phosphate group of ATP to specific amino acid side chains of substrate proteins. Serine, threonine, and tyrosine are the most commonly...
During phosphorylation, protein kinases transfer the terminal phosphate group of ATP to specific amino acid side chains of substrate proteins. Serine, threonine, and tyrosine are the most commonly...
50.2K
Protein Kinases and Phosphatases
13.1K
Proteins undergo chemical modifications that trigger changes in the charge, structure, and conformation of the proteins. Phosphorylation, acetylation, glycosylation, nitrosylation, ubiquitination, lipidation, methylation, and proteolysis are various protein modifications that regulate protein activity. Such modifications are usually enzyme-driven.
Protein kinases
Many proteins in the cell are regulated by phosphorylation, the addition of a phosphate group. A family of enzymes called kinases...
Protein kinases
Many proteins in the cell are regulated by phosphorylation, the addition of a phosphate group. A family of enzymes called kinases...
13.1K
Phosphoinositides and PIPs
8.5K
Phosphoinositides are a group of phospholipids containing a glycerol backbone with two fatty acid chains and a phosphate attached to a myoinositol sugar ring. The inositol head group extends into the cytoplasm, where it is modified by adding phosphate groups to form phosphatidylinositol phosphates or PIPs.
Different phosphoinositides are synthesized and recruited on the cytosolic face of the plasma membrane. The localization of specific phosphoinositides concentrated in separate membrane...
Different phosphoinositides are synthesized and recruited on the cytosolic face of the plasma membrane. The localization of specific phosphoinositides concentrated in separate membrane...
8.5K
The Phosphorus Cycle
36.7K
Unlike carbon, water, and nitrogen, phosphorus is not present in the atmosphere as a gas. Instead, most phosphorus in the ecosystem exists as compounds, such as phosphate ions (PO43-), found in soil, water, sediment and rocks. Phosphorus is often a limiting nutrient (i.e., in short supply). Consequently, phosphorus is added to most agricultural fertilizers, which can cause environmental problems related to runoff in aquatic ecosystems.
36.7K
Synthesis of Phosphatidylcholine in the ER Membrane
3.1K
The ER synthesizes lipids for building cell membranes and performing cellular functions such as energy storage and signaling. The lipid synthesis machinery embedded in the ER membrane primarily collects all reactants from the cytosol. Following synthesis, the secretory pathway and the ER contact sites distribute these lipids to other cellular organelles. Additionally, the energy-rich triacylglycerides are transported from the ER via lipid droplets.
The major components of all eukaryotic cell...
The major components of all eukaryotic cell...
3.1K
Protein Dynamics in Living Cells
2.1K
Different fluorescence-based techniques are used to study the protein dynamics in living cells. These techniques include FRAP, FRET, and PET.
Fluorescent recovery after photobleaching (FRAP) is a fluorescent-protein-based detection technique used to quantify protein movement rates within the cell. This method exposes a small portion of the cell to an intense laser beam. The laser beam causes permanent photobleaching of the fluorophore-tagged proteins in the exposed region. As the bleached...
Fluorescent recovery after photobleaching (FRAP) is a fluorescent-protein-based detection technique used to quantify protein movement rates within the cell. This method exposes a small portion of the cell to an intense laser beam. The laser beam causes permanent photobleaching of the fluorophore-tagged proteins in the exposed region. As the bleached...
2.1K


