7A4J

Aquifex aeolicus lumazine synthase-derived nucleocapsid variant NC-4

This is a non-PDB format compatible entry.

Summary for 7A4J

• Entry DOI: 10.2210/pdb7a4j/pdb
• EMDB information: 11631 11632 11633 11634 11635
• Descriptor: Antitermination protein N,6,7-dimethyl-8-ribityllumazine synthase,6,7-dimethyl-8-ribityllumazine synthase (1 entity in total)
• Functional Keywords: capsid, design, virus mimic, virus like particle
• Biological source: Escherichia virus lambda; More
• Total number of polymer chains: 240
• Total formula weight: 5154073.68

Authors

Tetter, S.,Hilvert, D. (deposition date: 2020-08-19, release date: 2021-06-02, Last modification date: 2024-05-01)

Primary citation

Tetter, S.,Terasaka, N.,Steinauer, A.,Bingham, R.J.,Clark, S.,Scott, A.J.P.,Patel, N.,Leibundgut, M.,Wroblewski, E.,Ban, N.,Stockley, P.G.,Twarock, R.,Hilvert, D.
Evolution of a virus-like architecture and packaging mechanism in a repurposed bacterial protein.
Science, 372:1220-1224, 2021

PubMed Abstract: Viruses are ubiquitous pathogens of global impact. Prompted by the hypothesis that their earliest progenitors recruited host proteins for virion formation, we have used stringent laboratory evolution to convert a bacterial enzyme that lacks affinity for nucleic acids into an artificial nucleocapsid that efficiently packages and protects multiple copies of its own encoding messenger RNA. Revealing remarkable convergence on the molecular hallmarks of natural viruses, the accompanying changes reorganized the protein building blocks into an interlaced 240-subunit icosahedral capsid that is impermeable to nucleases, and emergence of a robust RNA stem-loop packaging cassette ensured high encapsidation yields and specificity. In addition to evincing a plausible evolutionary pathway for primordial viruses, these findings highlight practical strategies for developing nonviral carriers for diverse vaccine and delivery applications.

PubMed: 34112695
DOI: 10.1126/science.abg2822

Experimental method

ELECTRON MICROSCOPY (3.04 Å)