Department of Biochemistry, University of Bayreuth, 95447 Bayreuth, Germany.
Department of Biochemistry, University of Bayreuth, 95447 Bayreuth, Germany.
Curr Opin Struct Biol. 2021 Jun;68:94-104. doi: 10.1016/j.sbi.2020.12.007. Epub 2021 Jan 13.
Proteins are chief actors in life that perform a myriad of exquisite functions. This diversity has been enabled through the evolution and diversification of protein folds. Analysis of sequences and structures strongly suggest that numerous protein pieces have been reused as building blocks and propagated to many modern folds. This information can be traced to understand how the protein world has diversified. In this review, we discuss the latest advances in the analysis of protein evolutionary units, and we use as a model system one of the most abundant and versatile topologies, the TIM-barrel fold, to highlight the existing common principles that interconnect protein evolution, structure, folding, function, and design.
蛋白质是生命中的主要演员，它们执行着无数精妙的功能。这种多样性是通过蛋白质折叠的进化和多样化实现的。序列和结构分析强烈表明，许多蛋白质片段被重复用作构建块，并传播到许多现代折叠中。这些信息可以追溯到了解蛋白质世界是如何多样化的。在这篇综述中，我们讨论了蛋白质进化单位分析的最新进展，并且我们使用最丰富和多功能的拓扑结构之一 TIM 桶折叠作为模型系统，突出了连接蛋白质进化、结构、折叠、功能和设计的现有共同原则。
