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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: 7bzt | ||||||
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タイトル | Cryo-EM structure of mature Coxsackievirus A10 in complex with KRM1 at pH 7.4 | ||||||
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![]() | VIRUS / Picornavirus / Coxsackievirus A10 / pH 7.4 / mature particle / KRM1 / complex | ||||||
機能・相同性 | ![]() Signaling by LRP5 mutants / Negative regulation of TCF-dependent signaling by WNT ligand antagonists / negative regulation of axon regeneration / cell communication / negative regulation of ossification / regulation of canonical Wnt signaling pathway / limb development / symbiont-mediated suppression of host cytoplasmic pattern recognition receptor signaling pathway via inhibition of MDA-5 activity / picornain 2A / symbiont-mediated suppression of host mRNA export from nucleus ...Signaling by LRP5 mutants / Negative regulation of TCF-dependent signaling by WNT ligand antagonists / negative regulation of axon regeneration / cell communication / negative regulation of ossification / regulation of canonical Wnt signaling pathway / limb development / symbiont-mediated suppression of host cytoplasmic pattern recognition receptor signaling pathway via inhibition of MDA-5 activity / picornain 2A / symbiont-mediated suppression of host mRNA export from nucleus / symbiont genome entry into host cell via pore formation in plasma membrane / picornain 3C / T=pseudo3 icosahedral viral capsid / TCF dependent signaling in response to WNT / host cell cytoplasmic vesicle membrane / negative regulation of canonical Wnt signaling pathway / cytoplasmic vesicle membrane / endocytosis involved in viral entry into host cell / Wnt signaling pathway / nucleoside-triphosphate phosphatase / protein complex oligomerization / monoatomic ion channel activity / RNA helicase activity / induction by virus of host autophagy / cysteine-type endopeptidase activity / RNA-directed RNA polymerase / viral RNA genome replication / virus-mediated perturbation of host defense response / RNA-dependent RNA polymerase activity / DNA-templated transcription / neuronal cell body / host cell nucleus / virion attachment to host cell / apoptotic process / structural molecule activity / ATP hydrolysis activity / proteolysis / RNA binding / ATP binding / membrane / metal ion binding / plasma 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 Å | ||||||
![]() | Cui, Y. / Peng, R. / Song, H. / Tong, Z. / Gao, G.F. / Qi, J. | ||||||
資金援助 | ![]()
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![]() | ![]() タイトル: Molecular basis of Coxsackievirus A10 entry using the two-in-one attachment and uncoating receptor KRM1. 著者: Yingzi Cui / Ruchao Peng / Hao Song / Zhou Tong / Xiao Qu / Sheng Liu / Xin Zhao / Yan Chai / Peiyi Wang / George F Gao / Jianxun Qi / ![]() 要旨: KREMEN1 (KRM1) has been identified as a functional receptor for Coxsackievirus A10 (CV-A10), a causative agent of hand-foot-and-mouth disease (HFMD), which poses a great threat to infants globally. ...KREMEN1 (KRM1) has been identified as a functional receptor for Coxsackievirus A10 (CV-A10), a causative agent of hand-foot-and-mouth disease (HFMD), which poses a great threat to infants globally. However, the underlying mechanisms for the viral entry process are not well understood. Here we determined the atomic structures of different forms of CV-A10 viral particles and its complex with KRM1 in both neutral and acidic conditions. These structures reveal that KRM1 selectively binds to the mature viral particle above the canyon of the viral protein 1 (VP1) subunit and contacts across two adjacent asymmetry units. The key residues for receptor binding are conserved among most KRM1-dependent enteroviruses, suggesting a uniform mechanism for receptor binding. Moreover, the binding of KRM1 induces the release of pocket factor, a process accelerated under acidic conditions. Further biochemical studies confirmed that receptor binding at acidic pH enabled CV-A10 virion uncoating in vitro. Taken together, these findings provide high-resolution snapshots of CV-A10 entry and identify KRM1 as a two-in-one receptor for enterovirus infection. | ||||||
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構造の表示
ムービー |
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構造ビューア | 分子: ![]() ![]() |
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PDBx/mmCIF形式 | ![]() | 203.2 KB | 表示 | ![]() |
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PDB形式 | ![]() | 165.7 KB | 表示 | ![]() |
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-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
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リンク
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集合体
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要素
-Capsid protein ... , 4種, 4分子 ABCD
#1: タンパク質 | 分子量: 33204.332 Da / 分子数: 1 / 由来タイプ: 天然 由来: (天然) ![]() ![]() 参照: UniProt: A0A0C5AWF6*PLUS |
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#2: タンパク質 | 分子量: 27783.105 Da / 分子数: 1 / 由来タイプ: 天然 由来: (天然) ![]() ![]() 参照: UniProt: G0YPI2 |
#3: タンパク質 | 分子量: 26187.623 Da / 分子数: 1 / 由来タイプ: 天然 由来: (天然) ![]() ![]() 参照: UniProt: G0YPI2 |
#4: タンパク質 | 分子量: 7464.104 Da / 分子数: 1 / 由来タイプ: 天然 由来: (天然) ![]() ![]() 参照: UniProt: G0YPI2 |
-タンパク質 / 非ポリマー / 糖 , 3種, 5分子 E![](data/chem/img/SPH.gif)
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#5: タンパク質 | 分子量: 41499.027 Da / 分子数: 1 / 由来タイプ: 組換発現 / 由来: (組換発現) ![]() ![]() |
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#6: 化合物 | ChemComp-SPH / |
#7: 糖 |
-詳細
研究の焦点であるリガンドがあるか | Y |
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配列の詳細 | The genome sequence of chain A have been deposit in GenBank: MT263729 |
-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: Coxsackievirus A10 / タイプ: VIRUS / Entity ID: #1-#5 / 由来: NATURAL |
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由来(天然) | 生物種: ![]() ![]() |
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: NO / 単離: STRAIN / タイプ: VIRION |
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 | 装置: FEI VITROBOT MARK IV / 凍結剤: ETHANE / 湿度: 100 % / 凍結前の試料温度: 277 K |
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電子顕微鏡撮影
実験機器 | ![]() モデル: Talos Arctica / 画像提供: FEI Company | ||||||||||||||||
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顕微鏡 | モデル: FEI TALOS ARCTICA | ||||||||||||||||
電子銃 | 電子線源: ![]() | ||||||||||||||||
電子レンズ | モード: BRIGHT FIELD | ||||||||||||||||
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解析
ソフトウェア | 名称: PHENIX / バージョン: 1.17.1_3660: / 分類: 精密化 | ||||||||||||||||||||||||
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CTF補正 | タイプ: PHASE FLIPPING AND AMPLITUDE CORRECTION | ||||||||||||||||||||||||
3次元再構成 | 解像度: 3 Å / 解像度の算出法: FSC 0.143 CUT-OFF / 粒子像の数: 28084 / 対称性のタイプ: POINT | ||||||||||||||||||||||||
拘束条件 |
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