Substrate-induced activation of a trapped IMC-medateed protein folding intermediate

Inouye M.; Shinde U.; Fu X.

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Substrate-induced activation of a trapped IMC-medateed protein folding intermediate

机译：基质诱导的被困IMC介导的蛋白折叠中间体的活化

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While several unfolded proteins acquire native structures through distinct folding intermediates, the physiological relevance and importance of such states in the folding kinetics remain controversial. The intramolecular chaperone (IMC) of subtilisin was used to trap a partially folded, stable crosslinked intermediate conformer (CLIC) through a disulfide bond between mutated IMC and subtilisin. The trapped CLIC contains non-native interactions. Here we show that CLIC can be induced into a catalytically active form by incubating it with small peptide substrates. The structure and catalytic properties of the activated crosslinked intermediate conformer (A-CLIC) differ from those of the fully folded enzyme in that A-CLIC lacks any endopeptidase activity toward a large protein substrate. Our results show that a disulfide-linked partially folded protein can be induced to acquire catalytic activity with a substrate specificity that is different from completely folded subtilisin, These results also suggest that protein folding intermediates may also participate in catalytic reactions. [References: 30]

机译：尽管几种未折叠的蛋白质通过独特的折叠中间体获得天然结构，但这种状态在折叠动力学中的生理相关性和重要性仍然存在争议。枯草杆菌蛋白酶的分子内分子伴侣（IMC）用于通过突变的IMC和枯草杆菌蛋白酶之间的二硫键捕获部分折叠的稳定交联的中间构象异构体（CLIC）。捕获的CLIC包含非本地交互。在这里，我们显示通过将CLIC与小的肽底物一起孵育可以将其诱导为催化活性形式。活化的交联的中间构象异构体（A-CLIC）的结构和催化特性与完全折叠的酶的结构和催化特性不同，因为A-CLIC对大蛋白底物缺乏任何内肽酶活性。我们的结果表明，可以诱导二硫键连接的部分折叠的蛋白质获得底物特异性不同于完全折叠的枯草杆菌蛋白酶的催化活性。这些结果还表明，蛋白质折叠的中间体也可能参与催化反应。 [参考：30]

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《Nature structural biology》 |2001年第4期|共5页
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Inouye M.; Shinde U.; Fu X.;
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1. Substrate-induced activation of a trapped IMC-medateed protein folding intermediate [J] . Inouye M., Shinde U., Fu X. Nature structural biology . 2001,第4期

机译：基质诱导的被困IMC介导的蛋白折叠中间体的活化
2. A partially folded intermediate species of the beta-sheet protein apo-pseudoazurin is trapped during proline-limited folding. [J] . Reader JS, Van-Nuland NA, Thompson GS, Protein Science: A Publication of the Protein Society . 2001,第6期

机译：β-折叠蛋白脱辅基伪天青素的部分折叠的中间物种在脯氨酸限制性折叠期间被捕获。
3. A kinetically trapped intermediate of FK506 binding protein forms in vitro: Chaperone machinery dominates protein folding in vivo [J] . Wear MA, Patterson A, Walkinshaw MD Protein Expression and Purification . 2007,第1期

机译：动力学上诱捕的FK506结合蛋白中间体在体外形成：伴侣蛋白分子在体内蛋白质折叠中占主导地位
4. Characterization of i-motif DNA kinetically trapped folding intermediates using nanoESI-TIMS-MS and molecular dynamics [C] . Alyssa Garabedian, David Butcher, Jennifer L. Lippens, ASMS Conference on Mass Spectrometry and Allied Topics . 2016

机译：使用纳米 - 矩阵和分子动力学的I-MOTIF DNA的表征I-MOTIF DNA动力学折叠中间体
5. Characterization of protein folding intermediates for delineation of folding pathways. [D] . Zheng, Zhongzhou. 2010

机译：蛋白质折叠中间体的表征，用于描绘折叠途径。
6. A partially folded intermediate species of the β-sheet protein apo-pseudoazurin is trapped during proline-limited folding [O] . John S. Reader, Nico A. J. Van Nuland, Gary S. Thompson, 2001

机译：β-折叠蛋白载脂蛋白假天青素的部分折叠中间物种在脯氨酸有限折叠过程中被捕获
7. NMR Analysis of the Conformational Properties of the Trapped on-pathway Folding Intermediate of the Bacterial Immunity Protein Im7 [O] . Whittaker, Sara B.-M., Spence, Graham R., Günter Grossmann, J., 2007

机译：捕获的细菌免疫蛋白Im7的途中折叠中间体构象性质的NMR分析。

Substrate-induced activation of a trapped IMC-medateed protein folding intermediate

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