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首页> 外文期刊>Journal of Molecular Biology >Generation of a highly active folding enzyme by combining a parvulin-type prolyl isomerase from sura with an unrelated chaperone domain
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Generation of a highly active folding enzyme by combining a parvulin-type prolyl isomerase from sura with an unrelated chaperone domain

机译：通过将来自苏拉的小肠蛋白型脯氨酰异构酶与无关的分子伴侣结构域结合，产生高活性的折叠酶

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摘要

Parvulins are small prolyl isomerases and serve as catalytic domains of folding enzymes. SurA (survival protein A) from the periplasm of Escherichia coli consists of an inactive (Par1) and an active (Par2) parvulin domain as well as a chaperone domain. In the absence of the chaperone domain, the folding activity of Par2 is virtually abolished. We created a chimeric protein by inserting the chaperone domain of SlyD, an unrelated folding enzyme from the FKBP family, into a loop of the isolated Par2 domain of SurA. This increased its folding activity 450-fold to a value higher than the activity of SurA, in which Par2 is linked with its natural chaperone domain. In the presence of both the natural and the foreign chaperone domain, the folding activity of Par2 was 1500-fold increased. Related and unrelated chaperone domains thus are similarly efficient in enhancing the folding activity of the prolyl isomerase Par2. A sequence analysis of various chaperone domains suggests that clusters of exposed methionine residues in mobile chain regions might be important for a generic interaction with unfolded protein chains. This binding is highly dynamic to allow frequent transfer of folding protein chains between chaperone and catalytic domains.
机译：细小蛋白是小的脯氨酰异构酶，并充当折叠酶的催化域。来自大肠杆菌周质的SurA（生存蛋白A）由一个无效的（Par1）和一个有效的（Par2）小肠蛋白域以及一个伴侣域组成。在没有伴侣域的情况下，Par2的折叠活性实际上被取消了。我们通过将SlyD的分子伴侣结构域（来自FKBP家族的不相关的折叠酶）插入SurA分离的Par2结构域的环中来创建嵌合蛋白。这将其折叠活性提高了450倍，使其值高于Sur2的活性，在SurA中，Par2与它的天然伴侣结构域相连。在天然和外来分子伴侣域的存在下，Par2的折叠活性提高了1500倍。因此，相关和不相关的伴侣结构域在增强脯氨酰异构酶Par2的折叠活性方面同样有效。各种分子伴侣结构域的序列分析表明，在移动链区域中暴露的蛋氨酸残基簇对于与未折叠的蛋白质链的通用相互作用可能很重要。这种结合是高度动态的，以允许折叠蛋白链在伴侣和催化结构域之间的频繁转移。

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