一个紧的结构的细胞染色体c被困在一个lysine-ligated状态:循环重新折叠和功能影响的合规交换机
Jeanine F Amacher1, Fangfang Zhong2, George P Lisi2
1†Department of Biochemistry, Geisel School of Medicine, Hanover, New Hampshire 03755, United States.
Journal of the American Chemical Society
|June 4, 2015
概括
细胞染色体c (cyt c) 的性形式发生结构变化,Lys取代Met80. 这种结构转变增强了其过氧化酶活性,支持其在亡中的作用.
科学领域:
- 生物化学 生物化学
- 结构生物学 结构生物学
- 细胞生物学 细胞生物学
背景情况:
- 细胞染色体c (cyt c) 在氧化酸化和亡中起作用.
- 性形式的cytc涉及lys取代met80,改变铁结合.
- 在连接体切换时细胞的形态变化尚未完全理解.
研究的目的:
- 为了阐明切换到Lys结合后cytc的结构重组.
- 研究这种结构变化对过氧化酶活性的功能后果.
- 在cytc中为lys结合提供热力学基础.
主要方法:
- 高分辨率的晶体结构测定Lys73结合细胞c.
- 化学衍生Cys78创建一个解决方案模仿.
- 用模型蛋白质进行酶活性测定和生物物理实验.
主要成果:
- 确定了Lys73结合细胞的紧结构,揭示了显著的血环境变化.
- 血红素协调循环重新折叠成β毛针,而血红素口袋的体积增加.
- 一种Cys78衍生模仿剂显示出增强的过氧化酶活性,支持 Lys-ligated cytc 在亡中的作用.
结论:
- 酸结合细胞表现出一个独特的,紧的结构,有一个扩大的血口袋.
- 这种结构性适应促进了心脂因相互作用,并在亡过程中增强了过氧化酶活性.
- 热力学研究解释了在特定的蛋白质支架扰动下切换到lys结合.
相关概念视频
Protein Folding
12.7K
Proteins are chains of amino acids linked together by peptide bonds. Upon synthesis, a protein folds into a three-dimensional conformation, critical to its biological function. Interactions between its constituent amino acids guide protein folding, and hence the protein structure is primarily dependent on its amino acid sequence.
Protein Structure Is Critical to Its Biological Function
Proteins perform a wide range of biological functions such as catalyzing chemical reactions, providing...
Protein Structure Is Critical to Its Biological Function
Proteins perform a wide range of biological functions such as catalyzing chemical reactions, providing...
12.7K
Protein Folding
131.1K
Overview
131.1K
Molecular Chaperones and Protein Folding
20.9K
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...
20.9K
Molecular Chaperones and Protein Folding
15.7K
15.7K
Export of Misfolded Proteins out of the ER
5.7K
After folding, the ER assesses the quality of secretory and membrane proteins. The correctly folded proteins are cleared by the calnexin cycle for transport to their final destination, while misfolded proteins are held back in the ER lumen. The ER chaperones attempt to unfold and refold the misfolded proteins but sometimes fail to achieve the correct native conformation. Such terminally misfolded proteins are then exported to the cytosol by ER-associated degradation or ERAD pathway for...
5.7K
Covalently Linked Protein Regulators
9.9K
Proteins can undergo many types of post-translational modifications, often in response to changes in their environment. These modifications play an important role in the function and stability of these proteins. Covalently linked molecules include functional groups, such as methyl, acetyl, and phosphate groups, and also small proteins, such as ubiquitin. There are around 200 different types of covalent regulators that have been identified.
These groups modify specific amino acids in a protein....
These groups modify specific amino acids in a protein....
9.9K


