8U1T

SARS-CoV-2 Envelope Protein Transmembrane Domain: Dimeric Structure Determined by Solid-State NMR

Summary for 8U1T

• Entry DOI: 10.2210/pdb8u1t/pdb
• NMR Information: BMRB: 31104
• Descriptor: Envelope small membrane protein (1 entity in total)
• Functional Keywords: sars-cov-2, envelope protein, e protein, transmembrane domain, membrane protein, pisema, pisa wheel, darr, viral protein
• Biological source: Severe acute respiratory syndrome coronavirus 2 (2019-nCoV, SARS-CoV-2)
• Total number of polymer chains: 2
• Total formula weight: 6177.61

Authors

Zhang, R.,Qin, H.,Prasad, R.,Fu, R.,Zhou, H.X.,Cross, T. (deposition date: 2023-09-02, release date: 2023-11-15, Last modification date: 2024-05-15)

Primary citation

Zhang, R.,Qin, H.,Prasad, R.,Fu, R.,Zhou, H.X.,Cross, T.A.
Dimeric Transmembrane Structure of the SARS-CoV-2 E Protein.
Commun Biol, 6:1109-1109, 2023

PubMed Abstract: The SARS-CoV-2 E protein is a transmembrane (TM) protein with its N-terminus exposed on the external surface of the virus. At debate is its oligomeric state, let alone its function. Here, the TM structure of the E protein is characterized by oriented sample and magic angle spinning solid-state NMR in lipid bilayers and refined by molecular dynamics simulations. This protein was previously found to be a pentamer, with a hydrophobic pore that appears to function as an ion channel. We identify only a front-to-front, symmetric helix-helix interface, leading to a dimeric structure that does not support channel activity. The two helices have a tilt angle of only 6°, resulting in an extended interface dominated by Leu and Val sidechains. While residues Val14-Thr35 are almost all buried in the hydrophobic region of the membrane, Asn15 lines a water-filled pocket that potentially serves as a drug-binding site. The E and other viral proteins may adopt different oligomeric states to help perform multiple functions.

PubMed: 37914906
DOI: 10.1038/s42003-023-05490-x

Experimental method

SOLID-STATE NMR