Department of Chemical Engineering, Columbia University, 500 W 120th Street, New York, NY 10027, USA.
Toxins (Basel). 2017 Sep 17;9(9):289. doi: 10.3390/toxins9090289.
The isolated Block V repeats-in-toxin (RTX) peptide domain of adenylate cyclase (CyaA) from reversibly folds into a β-roll secondary structure upon calcium binding. In this review, we discuss how the conformationally dynamic nature of the peptide is being engineered and employed as a switching mechanism to mediate different protein functions and protein-protein interactions. The peptide has been used as a scaffold for diverse applications including: a precipitation tag for bioseparations, a cross-linking domain for protein hydrogel formation and as an alternative scaffold for biomolecular recognition applications. Proteins and peptides such as the RTX domains that exhibit natural stimulus-responsive behavior are valuable building blocks for emerging synthetic biology applications.
可逆结合钙离子后,环化酶(CyaA)的分离 V 区重复入毒素(RTX)肽结构域会折叠成 β-发夹二级结构。在这篇综述中,我们讨论了如何对肽的构象动态性质进行工程改造,并将其作为开关机制来调节不同的蛋白质功能和蛋白质-蛋白质相互作用。该肽已被用作多种应用的支架,包括:生物分离的沉淀标签、蛋白质水凝胶形成的交联结构域以及生物分子识别应用的替代支架。具有天然刺激响应行为的蛋白质和肽(如 RTX 结构域)是新兴合成生物学应用的有价值的构建模块。