+
データを開く
-
基本情報
登録情報 | データベース: PDB / ID: 9n5m | |||||||||||||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
タイトル | The Turkey Parvovirus Capsid structure | |||||||||||||||||||||
![]() | VP2 | |||||||||||||||||||||
![]() | VIRUS / Capsid / Aveparvovirus / Turkey Parvovirus / cryo-EM / TuPV | |||||||||||||||||||||
機能・相同性 | Parvovirus coat protein VP2 / Parvovirus coat protein VP1/VP2 / Parvovirus coat protein VP2 / Capsid/spike protein, ssDNA virus / T=1 icosahedral viral capsid / structural molecule activity / VP2![]() | |||||||||||||||||||||
生物種 | ![]() | |||||||||||||||||||||
手法 | 電子顕微鏡法 / 単粒子再構成法 / クライオ電子顕微鏡法 / 解像度: 2.35 Å | |||||||||||||||||||||
![]() | Hsi, J. / Mietzsch, M. / McKenna, R. | |||||||||||||||||||||
資金援助 | ![]()
| |||||||||||||||||||||
![]() | ![]() タイトル: Birds of a feather flock together: structural characterization of red-crowned crane and turkey aveparvoviruses. 著者: Jane Hsi / Mario Mietzsch / Matthew Patney / Sunny Chen / Anjelique Sawh-Gopal / Paul Chipman / Robert McKenna / ![]() 要旨: The parvoviruses have non-enveloped = 1 icosahedral capsids that are ~25 nm in diameter, which package linear single-stranded DNA and infect a wide range of hosts. To date, parvoviruses affecting ...The parvoviruses have non-enveloped = 1 icosahedral capsids that are ~25 nm in diameter, which package linear single-stranded DNA and infect a wide range of hosts. To date, parvoviruses affecting birds have been identified in two genera: - and , and no capsid structures have been determined for any member of . This study investigates two bird viruses of this genus: red-crowned crane parvovirus (RCPV) and turkey parvovirus (TuPV). While the pathogenicity of RCPV is currently unknown, TuPV has been associated with gastrointestinal diseases, especially in juvenile birds. High-resolution structures of the RCPV and TuPV capsids were determined by cryo-electron microscopy at a resolution of 2.66 Å and 2.35 Å, respectively. A structural comparison of the RCPV and TuPV capsids shows that they exhibit many conserved features, such as a channel at the five-fold symmetry axis and surface depressions at the two-fold axis, as previously observed in parvoviruses from other genera. However, major structural differences were observed at the three-fold axes, with both RCPV and TuPV displaying recessed protrusions. In addition, terminal sialic acid was identified as a potential glycan receptor for RCPV. This study extends the architectural portfolio of structural parvovirology and will provide insights into parvoviral diversity and characterization of these viruses.IMPORTANCEThis study presents the capsid structures of two aveparvoviruses, red-crowned crane parvovirus (RCPV) and turkey parvovirus (TuPV), extending the structural repertoire of the . While the pathogenicity of RCPV is unknown, the red-crowned cranes are among the rarest crane species. To date, very few virological studies have been conducted for this rare avian species, and understanding their virome could contribute to conservation efforts. Additionally, several studies have previously suggested that TuPV is associated with cases of enteric disease syndrome. To date, no commercial antivirals or vaccines are available for TuPV. The structural characterization of its capsid may contribute toward the development of a treatment to control the spread of infection. | |||||||||||||||||||||
履歴 |
|
-
構造の表示
構造ビューア | 分子: ![]() ![]() |
---|
-
ダウンロードとリンク
-
ダウンロード
PDBx/mmCIF形式 | ![]() | 5.1 MB | 表示 | ![]() |
---|---|---|---|---|
PDB形式 | ![]() | 表示 | ![]() | |
PDBx/mmJSON形式 | ![]() | ツリー表示 | ![]() | |
その他 | ![]() |
-検証レポート
文書・要旨 | ![]() | 2 MB | 表示 | ![]() |
---|---|---|---|---|
文書・詳細版 | ![]() | 2.7 MB | 表示 | |
XML形式データ | ![]() | 785.7 KB | 表示 | |
CIF形式データ | ![]() | 1.2 MB | 表示 | |
アーカイブディレクトリ | ![]() ![]() | HTTPS FTP |
-関連構造データ
関連構造データ | ![]() 48927MC ![]() 9n5lC M: このデータのモデリングに利用したマップデータ C: 同じ文献を引用 ( |
---|---|
類似構造データ | 類似検索 - 機能・相同性 ![]() |
-
リンク
-
集合体
登録構造単位 | ![]()
|
---|---|
1 |
|
-
要素
#1: タンパク質 | 分子量: 60426.852 Da / 分子数: 60 / 由来タイプ: 組換発現 / 由来: (組換発現) ![]() 発現宿主: ![]() ![]() 参照: UniProt: D3X6X8 #2: 化合物 | ChemComp-MG / 研究の焦点であるリガンドがあるか | N | Has protein modification | N | |
---|
-実験情報
-実験
実験 | 手法: 電子顕微鏡法 |
---|---|
EM実験 | 試料の集合状態: PARTICLE / 3次元再構成法: 単粒子再構成法 |
-
試料調製
構成要素 | 名称: Turkey parvovirus 260 / タイプ: VIRUS / Entity ID: #1 / 由来: RECOMBINANT |
---|---|
由来(天然) | 生物種: ![]() |
由来(組換発現) | 生物種: ![]() ![]() 細胞: Sf9 |
ウイルスについての詳細 | 中空か: YES / エンベロープを持つか: NO / 単離: SPECIES / タイプ: VIRUS-LIKE PARTICLE |
緩衝液 | pH: 7.4 |
試料 | 包埋: NO / シャドウイング: NO / 染色: NO / 凍結: YES |
急速凍結 | 凍結剤: ETHANE |
-
電子顕微鏡撮影
顕微鏡 | モデル: JEOL CRYO ARM 300 |
---|---|
電子銃 | 電子線源: ![]() |
電子レンズ | モード: BRIGHT FIELD / 最大 デフォーカス(公称値): 1990 nm / 最小 デフォーカス(公称値): 950 nm |
撮影 | 電子線照射量: 50 e/Å2 / フィルム・検出器のモデル: GATAN K3 (6k x 4k) |
-
解析
EMソフトウェア | 名称: PHENIX / バージョン: 1.10-2155_2155 / カテゴリ: モデル精密化 | ||||||||||||||||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
CTF補正 | タイプ: NONE | ||||||||||||||||||||||||
3次元再構成 | 解像度: 2.35 Å / 解像度の算出法: FSC 0.143 CUT-OFF / 粒子像の数: 35131 / 対称性のタイプ: POINT | ||||||||||||||||||||||||
精密化 | 立体化学のターゲット値: REAL-SPACE (WEIGHTED MAP SUM AT ATOM CENTERS) | ||||||||||||||||||||||||
拘束条件 |
|