6ACD

Trypsin-cleaved and low pH-treated SARS-CoV spike glycoprotein and ACE2 complex, ACE2-free conformation with one RBD in up conformation

6ACD の概要

• エントリーDOI: 10.2210/pdb6acd/pdb
• EMDBエントリー: 9588 9589
• 分子名称: Spike glycoprotein (1 entity in total)
• 機能のキーワード: sars-cov, spike, glycoprotein, class i fusion protein, membrane fusion, viral protein
• 由来する生物種: Human SARS coronavirus (SARS-CoV)
• タンパク質・核酸の鎖数: 3
• 化学式量合計: 401290.27

構造登録者

Gui, M.,Song, W. (登録日: 2018-07-26, 公開日: 2018-08-08, 最終更新日: 2024-10-23)

主引用文献

Song, W.,Gui, M.,Wang, X.,Xiang, Y.
Cryo-EM structure of the SARS coronavirus spike glycoprotein in complex with its host cell receptor ACE2.
PLoS Pathog., 14:e1007236-e1007236, 2018

PubMed Abstract: The trimeric SARS coronavirus (SARS-CoV) surface spike (S) glycoprotein consisting of three S1-S2 heterodimers binds the cellular receptor angiotensin-converting enzyme 2 (ACE2) and mediates fusion of the viral and cellular membranes through a pre- to postfusion conformation transition. Here, we report the structure of the SARS-CoV S glycoprotein in complex with its host cell receptor ACE2 revealed by cryo-electron microscopy (cryo-EM). The complex structure shows that only one receptor-binding domain of the trimeric S glycoprotein binds ACE2 and adopts a protruding "up" conformation. In addition, we studied the structures of the SARS-CoV S glycoprotein and its complexes with ACE2 in different in vitro conditions, which may mimic different conformational states of the S glycoprotein during virus entry. Disassociation of the S1-ACE2 complex from some of the prefusion spikes was observed and characterized. We also characterized the rosette-like structures of the clustered SARS-CoV S2 trimers in the postfusion state observed on electron micrographs. Structural comparisons suggested that the SARS-CoV S glycoprotein retains a prefusion architecture after trypsin cleavage into the S1 and S2 subunits and acidic pH treatment. However, binding to the receptor opens up the receptor-binding domain of S1, which could promote the release of the S1-ACE2 complex and S1 monomers from the prefusion spike and trigger the pre- to postfusion conformational transition.

PubMed: 30102747
DOI: 10.1371/journal.ppat.1007236

実験手法

ELECTRON MICROSCOPY (3.9 Å)