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首页> 外文期刊>Journal of Molecular Biology >One Fold with Many Functions: The Evolutionary Relationships between TIM Barrel Families Based on their Sequences, Structures and Functions.
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One Fold with Many Functions: The Evolutionary Relationships between TIM Barrel Families Based on their Sequences, Structures and Functions.

机译：具有多种功能的一种折叠方式：TIM桶系列之间基于序列，结构和功能的进化关系。

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摘要

The eightfold (betaalpha) barrel structure, first observed in triose-phosphate isomerase, occurs ubiquitously in nature. It is nearly always an enzyme and most often involved in molecular or energy metabolism within the cell. In this review we bring together data on the sequence, structure and function of the proteins known to adopt this fold. We highlight the sequence and functional diversity in the 21 homologous superfamilies, which include 76 different sequence families. In many structures, the barrels are "mixed and matched" with other domains generating additional variety. Global and local structure-based alignments are used to explore the distribution of the associated functional residues on this common structural scaffold. Many of the substrates/co-factors include a phosphate moiety, which is usually but not always bound towards the C-terminal end of the sequence. Some, but not all, of these structures, exhibit a structurally conserved "phosphate binding motif". In contrast metal-ligating residues and catalytic residues are distributed along the sequence. However, we also found striking structural superposition of some of these residues. Lastly we consider the possible evolutionary relationships between these proteins, whose sequences are so diverse that even the most powerful approaches find few relationships, yet whose active sites all cluster at one end of the barrel. This extreme example of the "one fold-many functions" paradigm illustrates the difficulty of assigning function through a structural genomics approach for some folds.
机译：在三磷酸磷酸酯异构酶中首次发现的八倍（betaalpha）桶状结构在自然界普遍存在。它几乎总是一种酶，并且最常参与细胞内的分子或能量代谢。在这篇综述中，我们将已知采用这种折叠的蛋白质的序列，结构和功能的数据汇总在一起。我们重点介绍了21个同源超家族的序列和功能多样性，其中包括76个不同的序列家族。在许多结构中，桶与其他区域“混合并匹配”，从而产生其他变化。基于全局和局部结构的比对用于探索在该常见结构支架上相关功能残基的分布。许多底物/辅因子包括磷酸部分，其通常但不总是朝着序列的C-末端结合。这些结构中的一些但不是全部，表现出结构上保守的“磷酸盐结合基序”。相反，金属连接残基和催化残基沿序列分布。但是，我们还发现了其中一些残基的惊人结构重叠。最后，我们考虑了这些蛋白质之间可能的进化关系，这些蛋白质的序列是如此多样，以至于即使是最强大的方法也很少发现它们之间的关系，而其活性位点全部聚集在桶的一端。 “一个多折叠功能”范式的极端示例说明了通过结构基因组学方法对某些折叠进行功能分配的难度。

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