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8FDW

Cryo-EM structure of SARS-CoV-2 postfusion spike in membrane

8FDW の概要
エントリーDOI10.2210/pdb8fdw/pdb
EMDBエントリー29016
分子名称Spike protein S2, alpha-D-mannopyranose-(1-3)-alpha-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose, alpha-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose, ... (6 entities in total)
機能のキーワードviral protein
由来する生物種Severe acute respiratory syndrome coronavirus
タンパク質・核酸の鎖数3
化学式量合計215858.03
構造登録者
Zhang, J.,Shi, W.,Cai, Y.F.,Zhu, H.S.,Peng, H.Q.,Voyer, J.,Volloch, S.R.,Cao, H.,Mayer, M.L.,Song, K.K.,Xu, C.,Lu, J.M.,Chen, B. (登録日: 2022-12-05, 公開日: 2023-05-10, 最終更新日: 2024-11-06)
主引用文献Shi, W.,Cai, Y.,Zhu, H.,Peng, H.,Voyer, J.,Rits-Volloch, S.,Cao, H.,Mayer, M.L.,Song, K.,Xu, C.,Lu, J.,Zhang, J.,Chen, B.
Cryo-EM structure of SARS-CoV-2 postfusion spike in membrane.
Nature, 619:403-409, 2023
Cited by
PubMed Abstract: The entry of SARS-CoV-2 into host cells depends on the refolding of the virus-encoded spike protein from a prefusion conformation, which is metastable after cleavage, to a lower-energy stable postfusion conformation. This transition overcomes kinetic barriers for fusion of viral and target cell membranes. Here we report a cryogenic electron microscopy (cryo-EM) structure of the intact postfusion spike in a lipid bilayer that represents the single-membrane product of the fusion reaction. The structure provides structural definition of the functionally critical membrane-interacting segments, including the fusion peptide and transmembrane anchor. The internal fusion peptide forms a hairpin-like wedge that spans almost the entire lipid bilayer and the transmembrane segment wraps around the fusion peptide at the last stage of membrane fusion. These results advance our understanding of the spike protein in a membrane environment and may guide development of intervention strategies.
PubMed: 37285872
DOI: 10.1038/s41586-023-06273-4
主引用文献が同じPDBエントリー
実験手法
ELECTRON MICROSCOPY (2.9 Å)
構造検証レポート
Validation report summary of 8fdw
検証レポート(詳細版)ダウンロードをダウンロード

246905

件を2025-12-31に公開中

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