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首页> 外文期刊>Journal of Molecular Biology >Cooperation of the prolyl isomerase and chaperone activities of the protein folding catalyst SlyD.
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Cooperation of the prolyl isomerase and chaperone activities of the protein folding catalyst SlyD.

机译：蛋白质折叠催化剂SlyD的脯氨酰异构酶和伴侣活性的合作。

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摘要

The SlyD (sensitive to lysis D) protein of Escherichia coli is a folding enzyme with a chaperone domain and a prolyl isomerase domain of the FK506 binding protein type. Here we investigated how the two domains and their interplay are optimized for function in protein folding. Unfolded protein molecules initially form a highly dynamic complex with the chaperone domain of SlyD, and they are then transferred to the prolyl isomerase domain. The turnover number of the prolyl isomerase site is very high and guarantees that, after transfer, prolyl peptide bonds in substrate proteins are isomerized very rapidly. The Michaelis constant of catalyzed folding reflects the substrate affinity of the chaperone domain, and the turnover number is presumably determined by the rate of productive substrate transfer from the chaperone to the prolyl isomerase site and by the intrinsic propensity of the refolding protein chain to leave the active site with the native prolyl isomer. The efficiency of substrate transfer is high because dissociation from the chaperone site is very fast and because the two sites are close to each other. Protein molecules that left the prolyl isomerase site with an incorrect prolyl isomer can rapidly be re-bound by the chaperone domain because the association rate is very high as well.
机译：大肠杆菌的SlyD（对裂解D敏感）蛋白是一种折叠酶，具有FK506结合蛋白类型的分子伴侣结构域和脯氨酰异构酶结构域。在这里，我们研究了两个域及其相互作用如何优化蛋白质折叠功能。展开的蛋白质分子最初与SlyD的分子伴侣结构域形成高度动态的复合物，然后将其转移至脯氨酰异构酶结构域。脯氨酰异构酶位点的周转数非常高，并确保在转移后，底物蛋白中的脯氨酰肽键很快被异构化。催化折叠的米氏常数反映了分子伴侣结构域的底物亲和力，周转数大概是由生产性底物从分子伴侣转移至脯氨酰异构酶位点的速率以及再折叠蛋白链离开分子骨架的固有倾向性决定的。天然脯氨酰异构体的活性位点。底物转移的效率高，因为与伴侣位点的解离非常快，并且因为两个位点彼此靠近。伴有错误的脯氨酰异构体而留下脯氨酰异构酶位点的蛋白质分子也可以迅速被伴侣结构域重新结合，因为缔合率也很高。

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