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首页> 外文期刊>Acta crystallographica.Section D. Biological crystallography >The structure of a thermostable mutant of pro-papain reveals its activation mechanism
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The structure of a thermostable mutant of pro-papain reveals its activation mechanism

机译：的耐热性的突变体的结构pro-papain揭示其激活机制

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摘要

Papain is the archetype of a broad class of cysteine proteases (clan C1A) that contain a pro-peptide in the zymogen form which is required for correct folding and spatio-temporal regulation of proteolytic activity in the initial stages after expression. This study reports the X-ray structure of the zymogen of a thermostable mutant of papain at 2.6 ? resolution. The overall structure, in particular that of the mature part of the protease, is similar to those of other members of the family. The structure provides an explanation for the molecular basis of the maintenance of latency of the proteolytic activity of the zymogen by its pro-segment at neutral pH. The structural analysis, together with biochemical and biophysical studies, demonstrated that the pro-segment of the zymogen undergoes a rearrangement in the form of a structural loosening at acidic pH which triggers the proteolytic activation cascade. This study further explains the bimolecular stepwise autocatalytic activation mechanism by limited proteolysis of the zymogen of papain at the molecular level. The possible factors responsible for the higher thermal stability of the papain mutant have also been analyzed.
机译：木瓜蛋白酶是一类广泛的原型半胱氨酸蛋白酶(家族C1A)包含一个pro-peptide发酵菌形式中是必需的为正确的折叠和时空在最初的调节蛋白水解活动后阶段的表情。x射线结构发酵菌的耐热性的突变的木瓜蛋白酶在2.6吗?的结构,特别是成熟的一部分蛋白酶,类似于其他家庭的成员。解释的分子基础蛋白水解的维护的延迟活动由其pro-segment发酵菌的中性ph结构分析,在一起生物化学和生物物理的研究中,证明了pro-segment发酵菌经历一个重组的形式结构性放松在酸性pH值触发器蛋白水解激活级联。进一步解释了双分子的逐步催化活化机制有限木瓜蛋白酶的发酵菌的蛋白水解作用分子水平上。木瓜蛋白酶的热稳定性越高突变体也被分析。

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