Chemical Protein Synthesis Enabled Mechanistic Studies on the Molecular Recognition of K27-linked Ubiquitin Chains

文献类型： 外文期刊

第一作者： Pan, Man

作者： Pan, Man;Zheng, Qingyun;Qu, Qian;Wang, Tian;Liang, Lujun;Liu, Lei;Ding, Shan;Hong, Danning;Ren, Yujing;Mei, Ziqing;Zhang, Lujia;Chen, Chunlai;Pan, Man;Liu, Lei

作者机构：

关键词： chemical protein synthesis; native chemical ligation; smFRET; ubiquitin; x-ray crystallography

期刊名称：ANGEWANDTE CHEMIE-INTERNATIONAL EDITION （ 影响因子：15.336； 五年影响因子：14.205 ）

ISSN： 1433-7851

年卷期： 2019 年 58 卷 9 期

页码：

收录情况： SCI

摘要： New synthetic strategies that exploited the strengths of both chemoselective ligation and recombinant protein expression were developed to prepare K27 di-ubiquitins (diUb), which enabled mechanistic studies on the molecular recognition of K27-linked Ubs by single-molecule Forster resonance energy transfer (smFRET) and X-ray crystallography. The results revealed that free K27 diUb adopted a compact conformation, whereas upon binding to UCHL3, K27 diUb was remodeled to an open conformation. The K27 isopeptide bond remained rigidly buried inside the diUb moiety during binding, an interesting unique structural feature that may explain the distinctive biological function of K27 Ub chains.

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