7A4J の概要
| エントリーDOI | 10.2210/pdb7a4j/pdb |
| EMDBエントリー | 11631 11632 11633 11634 11635 |
| 分子名称 | Antitermination protein N,6,7-dimethyl-8-ribityllumazine synthase,6,7-dimethyl-8-ribityllumazine synthase (1 entity in total) |
| 機能のキーワード | capsid, design, virus mimic, virus like particle |
| 由来する生物種 | Escherichia virus lambda 詳細 |
| タンパク質・核酸の鎖数 | 240 |
| 化学式量合計 | 5154073.68 |
| 構造登録者 | |
| 主引用文献 | 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 Cited by 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: 34112695DOI: 10.1126/science.abg2822 主引用文献が同じPDBエントリー |
| 実験手法 | ELECTRON MICROSCOPY (3.04 Å) |
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