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Cellular Synthesis and X‐ray Crystal Structure of a Designed Protein Heterocatenane
Author(s) -
Liu Yajie,
Duan Zelin,
Fang Jing,
Zhang Fan,
Xiao Junyu,
Zhang WenBin
Publication year - 2020
Publication title -
angewandte chemie
Language(s) - English
Resource type - Journals
eISSN - 1521-3757
pISSN - 0044-8249
DOI - 10.1002/ange.202005490
Subject(s) - cleavage (geology) , intramolecular force , chemistry , catenane , topology (electrical circuits) , structural biology , crystal structure , protein crystallization , protein engineering , protein structure , crystallography , stereochemistry , enzyme , biochemistry , molecule , biology , crystallization , organic chemistry , mathematics , combinatorics , fracture (geology) , paleontology
Herein, we report the biosynthesis of protein heterocatenanes using a programmed sequence of multiple post‐translational processing events including intramolecular chain entanglement, in situ backbone cleavage, and spontaneous cyclization. The approach is general, autonomous, and can obviate the need for any additional enzymes. The catenane topology was convincingly proven using a combination of SDS‐PAGE, LC‐MS, size exclusion chromatography, controlled proteolytic digestion, and protein crystallography. The X‐ray crystal structure clearly shows two mechanically interlocked protein rings with intact folded domains. It opens new avenues in the nascent field of protein‐topology engineering.