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データを開く
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基本情報
登録情報 | データベース: PDB / ID: 7z51 | ||||||||||||||||||||||||||||||
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タイトル | Tick-borne encephalitis virus Kuutsalo-14 | ||||||||||||||||||||||||||||||
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![]() | VIRUS / virion / membrane protein / glycoprotein | ||||||||||||||||||||||||||||||
機能・相同性 | ![]() flavivirin / symbiont-mediated suppression of host JAK-STAT cascade via inhibition of STAT2 activity / symbiont-mediated suppression of host JAK-STAT cascade via inhibition of STAT1 activity / viral capsid / double-stranded RNA binding / nucleoside-triphosphate phosphatase / mRNA (guanine-N7)-methyltransferase / methyltransferase cap1 / clathrin-dependent endocytosis of virus by host cell / methyltransferase cap1 activity ...flavivirin / symbiont-mediated suppression of host JAK-STAT cascade via inhibition of STAT2 activity / symbiont-mediated suppression of host JAK-STAT cascade via inhibition of STAT1 activity / viral capsid / double-stranded RNA binding / nucleoside-triphosphate phosphatase / mRNA (guanine-N7)-methyltransferase / methyltransferase cap1 / clathrin-dependent endocytosis of virus by host cell / methyltransferase cap1 activity / mRNA 5'-cap (guanine-N7-)-methyltransferase activity / RNA helicase activity / protein dimerization activity / host cell perinuclear region of cytoplasm / host cell endoplasmic reticulum membrane / RNA helicase / symbiont-mediated suppression of host innate immune response / symbiont-mediated suppression of host type I interferon-mediated signaling pathway / symbiont-mediated activation of host autophagy / RNA-directed RNA polymerase / serine-type endopeptidase activity / viral RNA genome replication / RNA-directed RNA polymerase activity / fusion of virus membrane with host endosome membrane / viral envelope / virion attachment to host cell / host cell nucleus / virion membrane / structural molecule activity / ATP hydrolysis activity / proteolysis / extracellular region / ATP binding / metal ion binding / membrane 類似検索 - 分子機能 | ||||||||||||||||||||||||||||||
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: 3.3 Å | ||||||||||||||||||||||||||||||
![]() | Pulkkinen, L.I.A. / Barrass, S.V. / Anastasina, M. / Butcher, S.J. | ||||||||||||||||||||||||||||||
資金援助 | ![]() ![]()
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![]() | ![]() タイトル: Molecular Organisation of Tick-Borne Encephalitis Virus. 著者: Lauri I A Pulkkinen / Sarah V Barrass / Aušra Domanska / Anna K Överby / Maria Anastasina / Sarah J Butcher / ![]() ![]() 要旨: Tick-borne encephalitis virus (TBEV) is a pathogenic, enveloped, positive-stranded RNA virus in the family . Structural studies of flavivirus virions have primarily focused on mosquito-borne species, ...Tick-borne encephalitis virus (TBEV) is a pathogenic, enveloped, positive-stranded RNA virus in the family . Structural studies of flavivirus virions have primarily focused on mosquito-borne species, with only one cryo-electron microscopy (cryo-EM) structure of a tick-borne species published. Here, we present a 3.3 Å cryo-EM structure of the TBEV virion of the Kuutsalo-14 isolate, confirming the overall organisation of the virus. We observe conformational switching of the peripheral and transmembrane helices of M protein, which can explain the quasi-equivalent packing of the viral proteins and highlights their importance in stabilising membrane protein arrangement in the virion. The residues responsible for M protein interactions are highly conserved in TBEV but not in the structurally studied Hypr strain, nor in mosquito-borne flaviviruses. These interactions may compensate for the lower number of hydrogen bonds between E proteins in TBEV compared to the mosquito-borne flaviviruses. The structure reveals two lipids bound in the E protein which are important for virus assembly. The lipid pockets are comparable to those recently described in mosquito-borne Zika, Spondweni, Dengue, and Usutu viruses. Our results thus advance the understanding of tick-borne flavivirus architecture and virion-stabilising interactions. | ||||||||||||||||||||||||||||||
履歴 |
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構造の表示
構造ビューア | 分子: ![]() ![]() |
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ダウンロードとリンク
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ダウンロード
PDBx/mmCIF形式 | ![]() | 299.5 KB | 表示 | ![]() |
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PDB形式 | ![]() | 244.5 KB | 表示 | ![]() |
PDBx/mmJSON形式 | ![]() | ツリー表示 | ![]() | |
その他 | ![]() |
-検証レポート
アーカイブディレクトリ | ![]() ![]() | HTTPS FTP |
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-関連構造データ
関連構造データ | ![]() 14512MC 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 ( |
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類似構造データ | 類似検索 - 機能・相同性 ![]() |
電子顕微鏡画像生データ | ![]() Data size: 16.4 TB Data #1: Preparation 2 unaligned movies [micrographs - multiframe] Data #2: Preparation 3 unaligned movies [micrographs - multiframe]) |
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リンク
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集合体
登録構造単位 | ![]()
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要素
#1: タンパク質 | 分子量: 53558.270 Da / 分子数: 3 / 由来タイプ: 組換発現 由来: (組換発現) ![]() 株: Neudoerfl / 細胞株: SK-N-SH / 発現宿主: ![]() #2: タンパク質 | 分子量: 8311.854 Da / 分子数: 3 / 由来タイプ: 組換発現 由来: (組換発現) ![]() 株: Neudoerfl / 細胞株: SK-N-SH / 発現宿主: ![]() #3: 多糖 | #4: 化合物 | ChemComp-CPL / 研究の焦点であるリガンドがあるか | N | Has protein modification | Y | |
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-実験情報
-実験
実験 | 手法: 電子顕微鏡法 |
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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 |
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試料調製
構成要素 | 名称: Tick-borne encephalitis virus / タイプ: VIRUS 詳細: Virus was produced in SK-N-SH cells, purified, and inactivated with UV-C. Entity ID: #1-#2 / 由来: NATURAL |
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分子量 | 実験値: NO |
由来(天然) | 生物種: ![]() 株: Neudoerfl |
ウイルスについての詳細 | 中空か: NO / エンベロープを持つか: YES / 単離: SPECIES / タイプ: VIRION |
天然宿主 | 生物種: Homo sapiens |
緩衝液 | pH: 8.5 |
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 |
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電子顕微鏡撮影
実験機器 | ![]() モデル: Titan Krios / 画像提供: FEI Company |
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顕微鏡 | モデル: TFS KRIOS |
電子銃 | 電子線源: ![]() |
電子レンズ | モード: BRIGHT FIELD / 倍率(公称値): 81000 X / 最大 デフォーカス(公称値): 2700 nm / 最小 デフォーカス(公称値): 700 nm |
撮影 | 電子線照射量: 40 e/Å2 / フィルム・検出器のモデル: GATAN K3 (6k x 4k) |
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解析
CTF補正 | タイプ: PHASE FLIPPING AND AMPLITUDE CORRECTION |
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粒子像の選択 | 選択した粒子像数: 642026 |
対称性 | 点対称性: I (正20面体型対称) |
3次元再構成 | 解像度: 3.3 Å / 解像度の算出法: FSC 0.143 CUT-OFF / 粒子像の数: 119210 / 対称性のタイプ: POINT |