+データを開く
-基本情報
登録情報 | データベース: PDB / ID: 5g52 | ||||||
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タイトル | Crystallographic structure of full particle of Deformed Wing Virus | ||||||
要素 |
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キーワード | VIRUS (ウイルス) / PICORNAVIRALES (ピコルナウイルス目) / IFLAVIRIDAE / IFLAVIRUS / DWV CAPSID / P JELLYROLL / CATALYTIC SITE PROTEASE / LIPASE ESTERASE RECEPTO | ||||||
機能・相同性 | 機能・相同性情報 host cell membrane / カプシド / host cell cytoplasm / RNA helicase activity / viral RNA genome replication / cysteine-type endopeptidase activity / RNA-dependent RNA polymerase activity / DNA-templated transcription / structural molecule activity / タンパク質分解 ...host cell membrane / カプシド / host cell cytoplasm / RNA helicase activity / viral RNA genome replication / cysteine-type endopeptidase activity / RNA-dependent RNA polymerase activity / DNA-templated transcription / structural molecule activity / タンパク質分解 / RNA binding / ATP binding / 生体膜 / 細胞質 類似検索 - 分子機能 | ||||||
生物種 | DEFORMED WING VIRUS (ウイルス) | ||||||
手法 | X線回折 / シンクロトロン / 分子置換 / 解像度: 3.802 Å | ||||||
データ登録者 | Skubnik, K. / Novacek, J. / Fuzik, T. / Pridal, A. / Paxton, R. / Plevka, P. | ||||||
引用 | ジャーナル: Proc Natl Acad Sci U S A / 年: 2017 タイトル: Structure of deformed wing virus, a major honey bee pathogen. 著者: Karel Škubník / Jiří Nováček / Tibor Füzik / Antonín Přidal / Robert J Paxton / Pavel Plevka / 要旨: The worldwide population of western honey bees () is under pressure from habitat loss, environmental stress, and pathogens, particularly viruses that cause lethal epidemics. Deformed wing virus (DWV) ...The worldwide population of western honey bees () is under pressure from habitat loss, environmental stress, and pathogens, particularly viruses that cause lethal epidemics. Deformed wing virus (DWV) from the family , together with its vector, the mite , is likely the major threat to the world's honey bees. However, lack of knowledge of the atomic structures of iflaviruses has hindered the development of effective treatments against them. Here, we present the virion structures of DWV determined to a resolution of 3.1 Å using cryo-electron microscopy and 3.8 Å by X-ray crystallography. The C-terminal extension of capsid protein VP3 folds into a globular protruding (P) domain, exposed on the virion surface. The P domain contains an Asp-His-Ser catalytic triad that is, together with five residues that are spatially close, conserved among iflaviruses. These residues may participate in receptor binding or provide the protease, lipase, or esterase activity required for entry of the virus into a host cell. Furthermore, nucleotides of the DWV RNA genome interact with VP3 subunits. The capsid protein residues involved in the RNA binding are conserved among honey bee iflaviruses, suggesting a putative role of the genome in stabilizing the virion or facilitating capsid assembly. Identifying the RNA-binding and putative catalytic sites within the DWV virion structure enables future analyses of how DWV and other iflaviruses infect insect cells and also opens up possibilities for the development of antiviral treatments. | ||||||
履歴 |
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-構造の表示
構造ビューア | 分子: MolmilJmol/JSmol |
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-ダウンロードとリンク
-ダウンロード
PDBx/mmCIF形式 | 5g52.cif.gz | 185.3 KB | 表示 | PDBx/mmCIF形式 |
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PDB形式 | pdb5g52.ent.gz | 151.7 KB | 表示 | PDB形式 |
PDBx/mmJSON形式 | 5g52.json.gz | ツリー表示 | PDBx/mmJSON形式 | |
その他 | その他のダウンロード |
-検証レポート
アーカイブディレクトリ | https://data.pdbj.org/pub/pdb/validation_reports/g5/5g52 ftp://data.pdbj.org/pub/pdb/validation_reports/g5/5g52 | HTTPS FTP |
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-関連構造データ
-リンク
-集合体
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対称性 | 点対称性: (シェーンフリース記号: I (正20面体型対称)) | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
非結晶学的対称性 (NCS) | NCSドメイン:
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