CORRECT FOLDING OF CIRCULARLY PERMUTED VARIANTS OF A BETA-ALPHA-BARREL ENZYME INVIVO
CORRECT FOLDING OF CIRCULARLY PERMUTED VARIANTS OF A BETA-ALPHA-BARREL ENZYME INVIVO
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DOI：
10.1126/science.2643160
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发表时间：
1989-01-13
期刊：
影响因子：
56.9
通讯作者：
KIRSCHNER, K
中科院分区：
文献类型：
--
作者：
LUGER, K;HOMMEL, U;KIRSCHNER, K
蛋白质折叠中的一个重要问题是天然的氨基和羧基末端以及二级结构片段的给定顺序是否对蛋白质的稳定性和折叠途径至关重要。这里显示了单结构域β的基因的两个环状排列形式。α的桶酶可在大肠杆菌中表达。这些变体具有酶活性，并且通过几种结构和光谱标准几乎无法与原始酶区分，尽管产生了新的末端和表面环的裂解。这种新的遗传方法应该是有用的蛋白质折叠的研究在体外和体内。
An important question in protein folding is whether the natural amino and carboxyl termini and the given order of secondary structure segments are critical to the stability and to the folding pathway of proteins. Here it is shown that two circularly permuted versions of the gene of a single-domain .beta..alpha. barrel enzyme can be expressed in Escherichia coli. The variants are enzymically active and are practically indistinguishable from the original enzyme by several structural and spectroscopic criteria, despite the creation of new termini and the cleavage of a surface loop. This novel genetic approach should be useful for protein folding studies both in vitro and in vivo.