|Entry||Database: PDB / ID: 6ack|
|Title||Trypsin-cleaved and low pH-treated SARS-CoV spike glycoprotein and ACE2 complex, ACE2-bound conformation 3|
|Keywords||VIRAL PROTEIN/HYDROLASE / SARS-CoV / spike / glycoprotein / Class I fusion protein / membrane fusion / VIRAL PROTEIN / VIRAL PROTEIN-HYDROLASE complex|
|Function / homology|
Function and homology information
positive regulation of amino acid transport / angiotensin-converting enzyme 2 / tryptophan transport / angiotensin-mediated drinking behavior / positive regulation of gap junction assembly / positive regulation of cardiac muscle contraction / receptor biosynthetic process / regulation of systemic arterial blood pressure by renin-angiotensin / peptidyl-dipeptidase activity / exopeptidase activity ...positive regulation of amino acid transport / angiotensin-converting enzyme 2 / tryptophan transport / angiotensin-mediated drinking behavior / positive regulation of gap junction assembly / positive regulation of cardiac muscle contraction / receptor biosynthetic process / regulation of systemic arterial blood pressure by renin-angiotensin / peptidyl-dipeptidase activity / exopeptidase activity / regulation of vasoconstriction / regulation of blood vessel diameter / host cell endoplasmic reticulum-Golgi intermediate compartment membrane / angiotensin maturation / regulation of cytokine production / carboxypeptidase activity / receptor-mediated virion attachment to host cell / brush border membrane / metallocarboxypeptidase activity / regulation of cardiac conduction / dipeptidyl-peptidase activity / host cell surface receptor binding / endocytosis involved in viral entry into host cell / metallopeptidase activity / virus receptor activity / positive regulation of reactive oxygen species metabolic process / regulation of inflammatory response / regulation of cell population proliferation / fusion of virus membrane with host plasma membrane / endopeptidase activity / fusion of virus membrane with host endosome membrane / viral entry into host cell / viral envelope / membrane raft / host cell plasma membrane / virion membrane / pathogenesis / cell surface / extracellular space / zinc ion binding / extracellular exosome / integral component of membrane / extracellular region / identical protein binding / plasma membrane / cytoplasm
Angiotensin-converting enzyme / Spike glycoprotein N-terminal domain / Spike receptor binding domain / Spike glycoprotein / Spike receptor binding domain superfamily / Spike glycoprotein, N-terminal / Collectrin domain / Coronovirus spike glycoprotein, heptad repeat 2 domain / Spike receptor binding domain / Coronavirus S2 glycoprotein / Peptidase M2, peptidyl-dipeptidase A
Spike glycoprotein / Angiotensin-converting enzyme 2
|Biological species||Human SARS coronavirus|
Homo sapiens (human)
|Method||ELECTRON MICROSCOPY / single particle reconstruction / cryo EM / Resolution: 4.5 Å|
|Authors||Gui, M. / Song, W.|
|Citation||Journal: PLoS Pathog. / Year: 2018|
Title: Cryo-EM structure of the SARS coronavirus spike glycoprotein in complex with its host cell receptor ACE2.
Authors: Wenfei Song / Miao Gui / Xinquan Wang / Ye Xiang /
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 ...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.
SummaryFull reportAbout validation report
|Structure viewer||Molecule: |
Downloads & links
A: Spike glycoprotein
B: Spike glycoprotein
C: Spike glycoprotein
D: Angiotensin-converting enzyme 2
Mass: 133763.422 Da / Num. of mol.: 3
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Human SARS coronavirus / Gene: S, 2 / Production host: Spodoptera frugiperda (fall armyworm) / References: UniProt: P59594
Mass: 69982.562 Da / Num. of mol.: 1
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Homo sapiens (human) / Gene: ACE2, UNQ868/PRO1885 / Production host: Spodoptera frugiperda (fall armyworm)
References: UniProt: Q9BYF1, angiotensin-converting enzyme 2
|Experiment||Method: ELECTRON MICROSCOPY|
|EM experiment||Aggregation state: PARTICLE / 3D reconstruction method: single particle reconstruction|
|Molecular weight||Experimental value: NO|
|Buffer solution||pH: 5.8|
|Specimen||Embedding applied: NO / Shadowing applied: NO / Staining applied: NO / Vitrification applied: YES|
|Vitrification||Cryogen name: ETHANE|
-Electron microscopy imaging
Model: Titan Krios / Image courtesy: FEI Company
|Microscopy||Model: FEI TITAN KRIOS|
|Electron gun||Electron source: FIELD EMISSION GUN / Accelerating voltage: 300 kV / Illumination mode: FLOOD BEAM|
|Electron lens||Mode: BRIGHT FIELDBright-field microscopy|
|Image recording||Average exposure time: 8 sec. / Electron dose: 50 e/Å2 / Film or detector model: GATAN K2 SUMMIT (4k x 4k)|
|EM software||Name: RELION / Version: 1.4 / Category: 3D reconstruction|
|CTF correction||Type: PHASE FLIPPING AND AMPLITUDE CORRECTION|
|Symmetry||Point symmetry: C1 (asymmetric)|
|3D reconstruction||Resolution: 4.5 Å / Resolution method: FSC 0.143 CUT-OFF / Num. of particles: 56553 / Symmetry type: POINT|
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