4V7Q の概要
| エントリーDOI | 10.2210/pdb4v7q/pdb |
| EMDBエントリー | 5199 |
| 分子名称 | Core scaffold protein, Intermediate capsid protein VP6, Outer layer protein VP7, ... (7 entities in total) |
| 機能のキーワード | rotavirus, triple layered particle, near atomic resolution, vp2, vp6, vp4, vp7, double layered particle, de novo, infectious, virus, dlp, icosahedral virus |
| 由来する生物種 | Simian rotavirus A 詳細 |
| タンパク質・核酸の鎖数 | 31 |
| 化学式量合計 | 1440037.97 |
| 構造登録者 | Settembre, E.C.,Chen, J.Z.,Dormitzer, P.R.,Grigorieff, N.,Harrison, S.C. (登録日: 2010-05-13, 公開日: 2014-07-09, 最終更新日: 2024-10-16) |
| 主引用文献 | Settembre, E.C.,Chen, J.Z.,Dormitzer, P.R.,Grigorieff, N.,Harrison, S.C. Atomic model of an infectious rotavirus particle. Embo J., 30:408-416, 2011 Cited by PubMed Abstract: Non-enveloped viruses of different types have evolved distinct mechanisms for penetrating a cellular membrane during infection. Rotavirus penetration appears to occur by a process resembling enveloped-virus fusion: membrane distortion linked to conformational changes in a viral protein. Evidence for such a mechanism comes from crystallographic analyses of fragments of VP4, the rotavirus-penetration protein, and infectivity analyses of structure-based VP4 mutants. We describe here the structure of an infectious rotavirus particle determined by electron cryomicroscopy (cryoEM) and single-particle analysis at about 4.3 Å resolution. The cryoEM image reconstruction permits a nearly complete trace of the VP4 polypeptide chain, including the positions of most side chains. It shows how the two subfragments of VP4 (VP8(*) and VP5(*)) retain their association after proteolytic cleavage, reveals multiple structural roles for the β-barrel domain of VP5(*), and specifies interactions of VP4 with other capsid proteins. The virion model allows us to integrate structural and functional information into a coherent mechanism for rotavirus entry. PubMed: 21157433DOI: 10.1038/emboj.2010.322 主引用文献が同じPDBエントリー |
| 実験手法 | ELECTRON MICROSCOPY (3.8 Å) |
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