Disulfide-mediated conversion of 8-mer bowl-like protein architecture into three different nanocages
Jiachen Zang,
Hai Chen,
Xiaorong Zhang,
Chenxi Zhang,
Jing Guo,
Ming Du () and
Guanghua Zhao ()
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Jiachen Zang: China Agricultural University, Key Laboratory of Functional Dairy, Ministry of Education
Hai Chen: China Agricultural University, Key Laboratory of Functional Dairy, Ministry of Education
Xiaorong Zhang: China Agricultural University, Key Laboratory of Functional Dairy, Ministry of Education
Chenxi Zhang: China Agricultural University, Key Laboratory of Functional Dairy, Ministry of Education
Jing Guo: Tsinghua University
Ming Du: Dalian Polytechnic University
Guanghua Zhao: China Agricultural University, Key Laboratory of Functional Dairy, Ministry of Education
Nature Communications, 2019, vol. 10, issue 1, 1-11
Abstract:
Abstract Constructing different protein nanostructures with high-order discrete architectures by using one single building block remains a challenge. Here, we present a simple, effective disulfide-mediated approach to prepare a set of protein nanocages with different geometries from single building block. By genetically deleting an inherent intra-subunit disulfide bond, we can render the conversion of an 8-mer bowl-like protein architecture (NF-8) into a 24-mer ferritin-like nanocage in solution, while selective insertion of an inter-subunit disulfide bond into NF-8 triggers its conversion into a 16-mer lenticular nanocage. Deletion of the same intra-subunit disulfide bond and insertion of the inter-subunit disulfide bond results in the conversion of NF-8 into a 48-mer protein nanocage in solution. Thus, in the laboratory, simple mutation of one protein building block can generate three different protein nanocages in a manner that is highly reminiscent of natural pentamer building block originating from viral capsids that self-assemble into protein assemblies with different symmetries.
Date: 2019
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Persistent link: https://EconPapers.repec.org/RePEc:nat:natcom:v:10:y:2019:i:1:d:10.1038_s41467-019-08788-9
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DOI: 10.1038/s41467-019-08788-9
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