Dimeric Transmembrane Structure of the SARS-CoV-2 E Protein

被引：8
作者：
Zhang R. [1 ,2 ]
Qin H. [1 ]
Prasad R. [3 ]
Fu R. [2 ]
Zhou H.-X. [3 ,4 ]
Cross T.A. [1 ,2 ,5 ]
机构：
[1] Department of Chemistry and Biochemistry, Florida State University, Tallahassee, 32306, FL
[2] National High Magnetic Field Laboratory, Tallahassee, 32310, FL
[3] Department of Chemistry, University of Illinois Chicago, Chicago, 60607, IL
[4] Department of Physics, University of Illinois Chicago, Chicago, 60607, IL
[5] Institute of Molecular Biophysics, Florida State University, Tallahassee, 32306, FL
来源：
Communications Biology | / 6卷 / 1期
基金：
美国国家科学基金会; 美国国家卫生研究院;
关键词：
D O I：
10.1038/s42003-023-05490-x
中图分类号：
学科分类号：
摘要：
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. © 2023, The Author(s).
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