3GZU
VP7 recoated rotavirus DLP
3GZU の概要
| エントリーDOI | 10.2210/pdb3gzu/pdb |
| 関連するPDBエントリー | 3GZT |
| EMDBエントリー | 1571 1609 |
| 分子名称 | Inner capsid protein VP2, Intermediate capsid protein VP6, ZINC ION (3 entities in total) |
| 機能のキーワード | rotavirus, vp7, vp6, vp2, 7rp, dlp, capsid protein, metal-binding, virion, zinc, core protein, rna-binding, icosaderal virus, virus |
| 由来する生物種 | Rotavirus A (RV-A) 詳細 |
| タンパク質・核酸の鎖数 | 15 |
| 化学式量合計 | 770017.25 |
| 構造登録者 | Chen, J.Z.,Settembre, E.C.,Harrison, S.C.,Grigorieff, N. (登録日: 2009-04-07, 公開日: 2009-07-14, 最終更新日: 2024-02-21) |
| 主引用文献 | Chen, J.Z.,Settembre, E.C.,Aoki, S.T.,Zhang, X.,Bellamy, A.R.,Dormitzer, P.R.,Harrison, S.C.,Grigorieff, N. Molecular interactions in rotavirus assembly and uncoating seen by high-resolution cryo-EM. Proc.Natl.Acad.Sci.USA, 106:10644-10648, 2009 Cited by PubMed Abstract: Rotaviruses, major causes of childhood gastroenteritis, are nonenveloped, icosahedral particles with double-strand RNA genomes. By the use of electron cryomicroscopy and single-particle reconstruction, we have visualized a rotavirus particle comprising the inner capsid coated with the trimeric outer-layer protein, VP7, at a resolution (4 A) comparable with that of X-ray crystallography. We have traced the VP7 polypeptide chain, including parts not seen in its X-ray crystal structure. The 3 well-ordered, 30-residue, N-terminal "arms" of each VP7 trimer grip the underlying trimer of VP6, an inner-capsid protein. Structural differences between free and particle-bound VP7 and between free and VP7-coated inner capsids may regulate mRNA transcription and release. The Ca(2+)-stabilized VP7 intratrimer contact region, which presents important neutralizing epitopes, is unaltered upon capsid binding. PubMed: 19487668DOI: 10.1073/pnas.0904024106 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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