在蛋白质进化过程中,从循环中追踪结构域的诞生
M Fayez Aziz1, Fizza Mughal1, Gustavo Caetano-Anollés2,3
1Evolutionary Bioinformatics Laboratory, Department of Crop Sciences, University of Illinois, Urbana, IL, 61801, USA.
Scientific reports
|September 6, 2023
概括
蛋白质进化涉及结合循环支架来创建结构. 这项研究揭示了一个图形理论方法,以了解这些循环是如何形成一个不断演变的循环.
科学领域:
- 蛋白质进化和结构生物学.
- 计算生物学和生物信息学.
- 蛋白质结构的起源和发展.
背景情况:
- 蛋白质结构的起源和演变,特别是它们的循环支架和功能,仍然在很大程度上是未知的.
- 了解简单的结构图案如何组装成复杂的功能性蛋白质是分子生物学的一个关键挑战.
研究的目的:
- 用一种新的图形理论方法研究蛋白质域结构的进化途径.
- 阐明模块化和非模块化循环原型在折叠蛋白质结构形成中的相互作用.
- 重建"基本功能体" (EF) 的进化历史.
主要方法:
- 应用了一种新的图形理论方法来分析蛋白质域演变.
- 遗传学数据被用来创建时间表,并重新定位一个循环和域的双边网络.
- 早期P环和翼螺旋域的进化出现是使用AlphaFold2.2.建模的.
主要成果:
- 该研究确定了两个与"p-loop"和"翼螺旋"领域相关的功能创新的原始浪潮.
- 一个不断发展的"基本功能体" (EF) 被描绘在"布"中,显示结构和功能新性的出现和重用.
- 代谢途径在翻译功能之前扩展,并且观察到一个双重的沙钟招募模式.
- 阿尔法Fold2建模显示,古代领域的折叠结构迅速趋同,表明在循环中已经存在的"折叠词汇".
结论:
- 蛋白质域进化以循环和域的层次模块化为特征,由创新和再利用的循环驱动.
- 这些发现表明,蛋白环具有固有的"折叠词汇",这有助于折叠重定位和蛋白质设计.
- 这项研究为了解蛋白质结构和功能的进化轨迹提供了新的框架.
更多相关视频
12:04Interactome-Seq: A Protocol for Domainome Library Construction, Validation and Selection by Phage Display and Next Generation Sequencing
Published on: October 3, 2018
8.9K
11:14Combining Wet and Dry Lab Techniques to Guide the Crystallization of Large Coiled-coil Containing Proteins
Published on: January 6, 2017
8.0K
相关概念视频
Conservation of Protein Domains Over Different Proteins
10.9K
Protein domains are small structurally independent units that are part of a single amino acid chain. Although these domains are often structurally independent, they may rely on synergistic effects to perform their functions as part of a larger protein. Protein domains may be conserved within the same organism, as well as across different organisms.
A limited set of protein domains often duplicate and recombine during evolution. These domains can be organized in different combinations to...
A limited set of protein domains often duplicate and recombine during evolution. These domains can be organized in different combinations to...
10.9K
Conservation of Protein Domains
3.1K
3.1K
Conserved Binding Sites
4.2K
Many proteins’ biological role depends on their interactions with their ligands, small molecules that bind to specific locations on the protein known as ligand-binding sites. Ligand-binding sites are often conserved among homologous proteins as these sites are critical for protein function.
Binding sites are often located in large pockets, and if their location on a protein’s surface is unknown, it can be predicted using various approaches. The energetic method computationally...
Binding sites are often located in large pockets, and if their location on a protein’s surface is unknown, it can be predicted using various approaches. The energetic method computationally...
4.2K
Structural Protein Function
2.8K
2.8K
Three-Domain System of Life
49
Ribosomal RNA (rRNA) sequence analysis revealed three distinct groups of cells: eukaryotes, bacteria, and archaea. In 1978, Carl R. Woese proposed the concept of domains, a taxonomic level above kingdoms, to differentiate these groups. He suggested that archaea and bacteria, despite their similar appearance, represent separate domains. Domains differ in rRNA, membrane lipid structure, transfer RNA, and antibiotic sensitivity.In this classification, animals, plants, and fungi belong to the...
49
Protein Families
15.4K
Protein families are groups of homologous proteins; that is, they have similarities in amino acid sequences and three-dimensional structures. Protein families usually occur because of gene duplication, where an additional copy of a gene is inserted into the genome of an organism. Mutations that change the amino acids but still allow the protein to be properly synthesized, will lead to new protein family members. If these new proteins contain similar amino acids in key...
15.4K
