+
データを開く
-
基本情報
登録情報 | データベース: PDB / ID: 2xfb | ||||||
---|---|---|---|---|---|---|---|
タイトル | CHIKUNGUNYA E1 E2 ENVELOPE GLYCOPROTEINS FITTED IN SINDBIS VIRUS cryo- EM MAP | ||||||
![]() |
| ||||||
![]() | VIRUS / ALPHAVIRUS / RECEPTOR BINDING / MEMBRANE FUSION / ICOSAHEDRAL ENVELOPED VIRUS | ||||||
機能・相同性 | ![]() T=4 icosahedral viral capsid / host cell cytoplasm / symbiont entry into host cell / serine-type endopeptidase activity / fusion of virus membrane with host endosome membrane / virion attachment to host cell / host cell plasma membrane / structural molecule activity / virion membrane / proteolysis ...T=4 icosahedral viral capsid / host cell cytoplasm / symbiont entry into host cell / serine-type endopeptidase activity / fusion of virus membrane with host endosome membrane / virion attachment to host cell / host cell plasma membrane / structural molecule activity / virion membrane / proteolysis / identical protein binding / plasma membrane / cytoplasm 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: 9 Å | ||||||
![]() | Voss, J.E. / Vaney, M.C. / Duquerroy, S. / Rey, F.A. | ||||||
![]() | ![]() タイトル: Glycoprotein organization of Chikungunya virus particles revealed by X-ray crystallography. 著者: James E Voss / Marie-Christine Vaney / Stéphane Duquerroy / Clemens Vonrhein / Christine Girard-Blanc / Elodie Crublet / Andrew Thompson / Gérard Bricogne / Félix A Rey / ![]() 要旨: Chikungunya virus (CHIKV) is an emerging mosquito-borne alphavirus that has caused widespread outbreaks of debilitating human disease in the past five years. CHIKV invasion of susceptible cells is ...Chikungunya virus (CHIKV) is an emerging mosquito-borne alphavirus that has caused widespread outbreaks of debilitating human disease in the past five years. CHIKV invasion of susceptible cells is mediated by two viral glycoproteins, E1 and E2, which carry the main antigenic determinants and form an icosahedral shell at the virion surface. Glycoprotein E2, derived from furin cleavage of the p62 precursor into E3 and E2, is responsible for receptor binding, and E1 for membrane fusion. In the context of a concerted multidisciplinary effort to understand the biology of CHIKV, here we report the crystal structures of the precursor p62-E1 heterodimer and of the mature E3-E2-E1 glycoprotein complexes. The resulting atomic models allow the synthesis of a wealth of genetic, biochemical, immunological and electron microscopy data accumulated over the years on alphaviruses in general. This combination yields a detailed picture of the functional architecture of the 25 MDa alphavirus surface glycoprotein shell. Together with the accompanying report on the structure of the Sindbis virus E2-E1 heterodimer at acidic pH (ref. 3), this work also provides new insight into the acid-triggered conformational change on the virus particle and its inbuilt inhibition mechanism in the immature complex. #1: ![]() タイトル: Mapping the structure and function of the E1 and E2 glycoproteins in alphaviruses. 著者: Suchetana Mukhopadhyay / Wei Zhang / Stefan Gabler / Paul R Chipman / Ellen G Strauss / James H Strauss / Timothy S Baker / Richard J Kuhn / Michael G Rossmann / ![]() 要旨: The 9 A resolution cryo-electron microscopy map of Sindbis virus presented here provides structural information on the polypeptide topology of the E2 protein, on the interactions between the E1 and ...The 9 A resolution cryo-electron microscopy map of Sindbis virus presented here provides structural information on the polypeptide topology of the E2 protein, on the interactions between the E1 and E2 glycoproteins in the formation of a heterodimer, on the difference in conformation of the two types of trimeric spikes, on the interaction between the transmembrane helices of the E1 and E2 proteins, and on the conformational changes that occur when fusing with a host cell. The positions of various markers on the E2 protein established the approximate topology of the E2 structure. The largest conformational differences between the icosahedral surface spikes at icosahedral 3-fold and quasi-3-fold positions are associated with the monomers closest to the 5-fold axes. The long E2 monomers, containing the cell receptor recognition motif at their extremities, are shown to rotate by about 180 degrees and to move away from the center of the spikes during fusion. | ||||||
履歴 |
|
-
構造の表示
ムービー |
![]() |
---|---|
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 | ![]() | 548 KB | 表示 | ![]() |
---|---|---|---|---|
PDB形式 | ![]() | 462.5 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 |
---|
-関連構造データ
-
リンク
-
集合体
登録構造単位 | ![]()
|
---|---|
1 | ![]()
| x 60
2 |
|
3 | ![]()
| x 5
4 | ![]()
| x 6
5 | ![]()
|
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)) |
-
要素
#1: タンパク質 | 分子量: 42554.148 Da / 分子数: 4 / 断片: ECTODOMAIN, RESIDUES 810-1248 / 由来タイプ: 組換発現 由来: (組換発現) ![]() ![]() 株: 05-115 / プラスミド: PMRBIP/V5HISA 発現宿主: ![]() ![]() 株 (発現宿主): SCHNEIDER 2 / 参照: UniProt: Q1H8W5 #2: タンパク質 | 分子量: 37621.594 Da / 分子数: 4 / 断片: ECTODOMAIN, RESIDUES 326-748 / 由来タイプ: 組換発現 由来: (組換発現) ![]() ![]() 株: 05-115 / プラスミド: PMRBIP/V5HISA 発現宿主: ![]() ![]() 株 (発現宿主): SCHNEIDER 2 / 参照: UniProt: Q1H8W5 |
---|
-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: Sindbis virus / タイプ: VIRUS |
---|---|
緩衝液 | pH: 7.4 / 詳細: 20 mM Tris-Cl, 200 mM NaCl, 0.1 mM EDTA |
試料 | 包埋: NO / シャドウイング: NO / 染色: NO / 凍結: YES |
試料支持 | 詳細: OTHER |
急速凍結 | 装置: HOMEMADE PLUNGER / 凍結剤: ETHANE |
-
電子顕微鏡撮影
顕微鏡 | モデル: FEI/PHILIPS CM200T / 日付: 2000年6月21日 |
---|---|
電子銃 | 電子線源: OTHER / 加速電圧: 100 kV / 照射モード: FLOOD BEAM |
電子レンズ | モード: OTHER / 倍率(公称値): 38000 X / 最大 デフォーカス(公称値): 2580 nm / 最小 デフォーカス(公称値): 1100 nm |
撮影 | 電子線照射量: 18 e/Å2 / フィルム・検出器のモデル: KODAK SO-163 FILM |
放射波長 | 相対比: 1 |
-
解析
対称性 | 点対称性: I (正20面体型対称) | ||||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|---|
3次元再構成 | 解像度: 9 Å / 粒子像の数: 7085 詳細: THE COMPLETE PARTICLE IS GENERATED BY BIOMT MATRICES. THE FIT WAS GENERATED WITH URO IN SINDBIS CRYO-EM MAP EMDB-1121 USING PDB ENTRY 3N40. 対称性のタイプ: POINT | ||||||||||||
原子モデル構築 | PDB-ID: 3N40 | ||||||||||||
精密化 | 最高解像度: 9 Å | ||||||||||||
精密化ステップ | サイクル: LAST / 最高解像度: 9 Å
|