Viral envelope

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The hull of the virus is made up of a double membrane of lipids (shown in grey) from the host cell in which the virus was made.

The water-loving (hydrophilic) parts of the lipids face outside, while the water-adverse (hydrophobic) parts face to the inside of the membrane. This arrangement easily explains why the virus can be destroyed by soap: soap dissolves bi-lipidic membranes.

You want to know more?

See https://pdb101.rcsb.org/learn/videos/fighting-coronavirus-with-soap

In addition to the Spike protein, there are two more proteins embedded in the bilipidic membrane, the membrane protein and the envelope protein.

The membrane protein plays an important role in the assembly of the viral macromolecules in the host cell (Ensuring everything is packed correctly to be functional). To date no atomic structure has been determined of the membrane protein.

The small envelope (E) protein also appears to play a major role in the formation of virions. Without the E protein, fewer viruses are produced and are less virulent. The E protein forms pentameric pores in the host cell membranes which act as ion transporters (yellow) – if they actually exist on the viral hull is unclear.

Image
PDB
Protein
Description
Preview
Github-Link
Refinement
Method
Resolution
R(work)
R(free)
Virus
preview of 2mm4
2mm4
protein_e
This NMR structure is a monomer of the SARS-CoV envelope protein (E). It completely covers the transmembrane domain and the C- and N-terminus partly. The structure is involved in membrane curvature, membrane scission, and viral assembly.
3D
Preview
SOLUTION NMR
null Å
---
---
SARS-CoV
preview of 5x29
5x29
protein_e
This NMR structure is an oligomer of the envelope protein (E) of SARS-CoV. The structure is a pentamer of five identical monomers. It covers the transmembrane domain and the C- and N-terminus partly. This structure functions as a membrane-anchored ion channel.
3D
Preview
SOLUTION NMR
null Å
---
---
SARS-CoV
preview of 5xer
5xer
protein_e
This NMR structure exhibits a short part of the monomeric envelope protein (E) of SARS-CoV. The structure covers 9 residues of the short α-helix in the C-terminus. It is proposed to be in dynamic equilibrium with an β-coil-β-motif and may work as a Golgi targeting signal.
3D
Preview
SOLUTION NMR
null Å
---
---
SARS-CoV
preview of 5xes
5xes
protein_e
This NMR structure exhibits a short part of the monomeric envelope protein (E) of SARS-CoV. The structure covers 9 residues of the short α-helix in the C-terminus. It is proposed to be in dynamic equilibrium with an β-coil-β-motif and may work as a Golgi targeting signal. 5xes has a better overall quality than 5xer
3D
Preview
SOLUTION NMR
null Å
---
---
SARS-CoV
preview of 7k3g
7k3g
protein_e
The pentameric structure of the SARS-CoV-2 envelope protein transmembrane domain. The structure was determined by solid-state NMR. The e protein is important for the virus pathogenicity.
3D
Preview
SOLID-STATE NMR
null Å
---
---
SARS-CoV-2
preview of 7ntk
7ntk
protein_e
3D
Preview
X-RAY DIFFRACTION
1.9 Å
0.1957
0.2287
SARS-CoV-2
preview of 7m4r
7m4r
protein_e
3D
Preview
ELECTRON MICROSCOPY
3.65 Å
---
---
SARS-CoV-2
preview of 7ntj
7ntj
protein_e
3D
Preview
X-RAY DIFFRACTION
1.74 Å
0.1517
0.1852
SARS-CoV
preview of 7qcs
7qcs
protein_e
3D
Preview
X-RAY DIFFRACTION
2.804 Å
0.2633
0.3049
SARS-CoV-2
preview of 7qcr
7qcr
protein_e
3D
Preview
X-RAY DIFFRACTION
2.28 Å
0.2208
0.2523
SARS-CoV-2
preview of 7qct
7qct
protein_e
3D
Preview
X-RAY DIFFRACTION
3.197 Å
0.2281
0.2395
SARS-CoV-2
preview of 7tuq
7tuq
protein_e
3D
Preview
X-RAY DIFFRACTION
2.68 Å
0.216
0.276
SARS-CoV-2
preview of 7tv0
7tv0
protein_e
3D
Preview
X-RAY DIFFRACTION
2.5 Å
0.2428
0.2922
SARS-CoV-2
cross