Structure and dynamics of a primordial catalytic fold generated by in vitro evolution.

Structure and dynamics of a primordial catalytic fold generated by in vitro evolution.
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DOI:
10.1038/nchembio.1138
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发表时间:
2013-02
影响因子:
14.8
通讯作者:
Seelig B
Seelig B
中科院分区:
生物学1区
文献类型:
--
作者:
Chao FA;Morelli A;Haugner JC 3rd;Churchfield L;Hagmann LN;Shi L;Masterson LR;Sarangi R;Veglia G;Seelig B

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设计能够进行化学催化的功能蛋白质支架是酶设计的主要挑战。从非催化蛋白质支架出发,我们最近通过体外定向进化产生了一种新的RNA连接酶。这种人工酶失去了原来的折叠,并采用了一种全新的结构,具有显着增强的构象动力学,表明具有适当灵活性的原始折叠足以进行酶功能。
Engineering functional protein scaffolds capable of carrying out chemical catalysis is a major challenge in enzyme design. Starting from a non-catalytic protein scaffold, we recently generated a novel RNA ligase by in vitro directed evolution. This artificial enzyme lost its original fold and adopted an entirely novel structure with dramatically enhanced conformational dynamics, demonstrating that a primordial fold with suitable flexibility is sufficient to carry out enzymatic function.
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