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- W2596288825 abstract "Correct outer protein shell assembly is a prerequisite for virion infectivity in many multi-shelled dsRNA viruses. In the prototypic dsRNA bacteriophage φ6, the assembly reaction is promoted by calcium ions but its biomechanics remain poorly understood. Here, we describe the near-atomic resolution structure of the φ6 double-shelled particle. The outer T=13 shell protein P8 consists of two alpha-helical domains joined by a linker, which allows the trimer to adopt either a closed or an open conformation. The trimers in an open conformation swap domains with each other. Our observations allow us to propose a mechanistic model for calcium concentration regulated outer shell assembly. Furthermore, the structure provides a prime exemplar of bona fide domain-swapping. This leads us to extend the theory of domain-swapping from the level of monomeric subunits and multimers to closed spherical shells, and to hypothesize a mechanism by which closed protein shells may arise in evolution." @default.
- W2596288825 created "2017-03-23" @default.
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- W2596288825 date "2017-03-13" @default.
- W2596288825 modified "2023-10-13" @default.
- W2596288825 title "Double-stranded RNA virus outer shell assembly by bona fide domain-swapping" @default.
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- W2596288825 doi "https://doi.org/10.1038/ncomms14814" @default.
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