Journal
ANGEWANDTE CHEMIE-INTERNATIONAL EDITION
Volume 59, Issue 37, Pages 16122-16127Publisher
WILEY-V C H VERLAG GMBH
DOI: 10.1002/anie.202005490
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Funding
- National Natural Science Foundation of China [21925102, 21991132, 21674003]
- National Key Research and Development Program of China [2017YFA0505200]
- Beijing National Laboratory for Molecular Sciences [BNLMS-CXXM-202006]
- Clinical Medicine Plus X project of Peking University, Fundamental Research Funds for the Central Universities
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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 inter-locked protein rings with intact folded domains. It opens new avenues in the nascent field of protein-topology engineering.
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