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

被引：63

作者：

Pan, Man ^{[1
,4
]}

Zheng, Qingyun ^{[1
]}

Ding, Shan ^{[2
]}

Zhang, Lujia ^{[3
]}

Qu, Qian ^{[1
]}

Wang, Tian ^{[1
]}

Hong, Danning ^{[2
]}

Ren, Yujing ^{[2
]}

Liang, Lujun ^{[1
]}

Chen, Chunlai ^{[3
]}

Mei, Ziqing ^{[2
]}

Liu, Lei ^{[1
,4
]}

机构：

[1] Tsinghua Univ, Tsinghua Peking Ctr Life Sci, MOE Key Lab Bioorgan Phosphorus Chem & Chem Biol, Dept Chem,Ctr Synthet & Syst Biol, Beijing 100084, Peoples R China

[2] Chinese Acad Agr Sci, Biotechnol Res Inst, Beijing 100081, Peoples R China

[3] Tsinghua Univ, Sch Life Sci, Beijing Adv Innovat Ctr Struct Biol, Beijing 100084, Peoples R China

[4] Tsinghua Univ, Grad Sch Shenzen, Key Lab Chem Biol, State Key Lab Chem Oncogen, Shenzhen 518055, Guangdong, Peoples R China

来源：

ANGEWANDTE CHEMIE-INTERNATIONAL EDITION | 2019年 / 58卷 / 09期

关键词：

chemical protein synthesis; native chemical ligation; smFRET; ubiquitin; x-ray crystallography; CYSTEINE; DEHYDROALANINE; PEPTIDES; LINKAGE;

D O I：

10.1002/anie.201810814

中图分类号：

O6 [化学];

学科分类号：

0703 ;

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.

引用

页码：2627 / 2631

页数：5

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