3GZT
VP7 recoated rotavirus DLP
3GZT の概要
エントリーDOI | 10.2210/pdb3gzt/pdb |
関連するPDBエントリー | 3GZU |
EMDBエントリー | 1571 1609 |
分子名称 | Outer capsid glycoprotein VP7, 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose, CALCIUM ION (3 entities in total) |
機能のキーワード | rotavirus, vp7, vp6, vp2, 7rp, dlp, icosahedral virus, capsid protein, disulfide bond, endoplasmic reticulum, glycoprotein, membrane, transmembrane, virion, virus |
由来する生物種 | Rhesus rotavirus (RV-A) |
細胞内の位置 | Virion (By similarity): P12476 |
タンパク質・核酸の鎖数 | 13 |
化学式量合計 | 380345.42 |
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: 2024-10-30) |
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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