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Chemical Protein Synthesis Enabled Mechanistic Studies on the Molecular Recognition of K27‐linked Ubiquitin Chains
Author(s) -
Pan Man,
Zheng Qingyun,
Ding Shan,
Zhang Lujia,
Qu Qian,
Wang Tian,
Hong Danning,
Ren Yujing,
Liang Lujun,
Chen Chunlai,
Mei Ziqing,
Liu Lei
Publication year - 2019
Publication title -
angewandte chemie international edition
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 5.831
H-Index - 550
eISSN - 1521-3773
pISSN - 1433-7851
DOI - 10.1002/anie.201810814
Subject(s) - chemistry , moiety , ubiquitin , stereochemistry , biochemistry , gene
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 Förster 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.