Tandem-repeat proteins conformational mechanics are optimized to facilitate functional interactions and complexations
Tandem-repeat proteins conformational mechanics are optimized to facilitate functional interactions and complexations
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DOI：
10.1016/j.sbi.2023.102744
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发表时间：
2023-12-21
影响因子：
6.8
通讯作者：
Bahar，Ivet
中科院分区：
文献类型：
--
作者：
Ventura，Carlos;Banerjee，Anupam;Bahar，Ivet
串联重复蛋白的结构与球形蛋白的结构不同。单个模块，每个包含20-40个残基的小结构基序，以准一维的方式排列，形成醒目的、细长的、马蹄形和超螺旋结构，仅通过短程相互作用稳定。重复序列的弹簧形状指向了弹性的作用模式，这些蛋白质作为适配器分子或“枢纽”发挥作用，在不同的生物环境中在多亚基组装内传播信号。这种灵活性从不同复合体中串联重复蛋白结构的戏剧性变化中可见一斑。在这里，利用计算分析，我们演示了仅仅一个或几个全球运动重述这些结构的惊人能力。这些发现表明，重复阵列的机制是如何通过其独特的体系结构来强劲实现的。因此，重复的结构已经通过进化进行了优化，以支持运动的功能模式。实现功能转换的全球运动可以在http://bahargroup.org/tr_web.上完全可视化
The architectures of tandem-repeat proteins are distinct from those of globular proteins. Individual modules, each comprising small structural motifs of 20–40 residues, are arrayed in a quasi one-dimensional fashion to form striking, elongated, horseshoe-like, and superhelical architectures, stabilized solely by short–range interaction. The spring-like shapes of repeat arrays point to elastic modes of action, and these proteins function as adapter molecules or ‘hubs,’ propagating signals within multi-subunit assemblies in diverse biological contexts. This flexibility is apparent in the dramatic variability observed in the structures of tandem-repeat proteins in different complexes. Here, using computational analysis, we demonstrate the striking ability of just one or a few global motions to recapitulate these structures. These findings show how the mechanics of repeat arrays are robustly enabled by their unique architecture. Thus, the repeating architecture has been optimized by evolution to favor functional modes of motions. The global motions enabling functional transitions can be fully visualized at http://bahargroup.org/tr_web.