Protein Structure and Folding
Structure of a Conserved Golgi Complex-targeting Signal in Coronavirus Envelope Proteins

https://doi.org/10.1074/jbc.M114.560094Get rights and content
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Coronavirus envelope (CoV E) proteins are ∼100-residue polypeptides with at least one channel-forming α-helical transmembrane (TM) domain. The extramembrane C-terminal tail contains a completely conserved proline, at the center of a predicted β-coil-β motif. This hydrophobic motif has been reported to constitute a Golgi-targeting signal or a second TM domain. However, no structural data for this or other extramembrane domains in CoV E proteins is available. Herein, we show that the E protein in the severe acute respiratory syndrome virus has only one TM domain in micelles, whereas the predicted β-coil-β motif forms a short membrane-bound α-helix connected by a disordered loop to the TM domain. However, complementary results suggest that this motif is potentially poised for conformational change or in dynamic exchange with other conformations.

Analytical Ultracentrifugation
Nuclear Magnetic Resonance (NMR)
Protein Structure
Structural Biology
Viral Protein
Virus Assembly
Golgi Targeting
SARS
Coronavirus
Envelope Protein

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1

Both authors contributed equally to this work.

The atomic coordinates and structure factors (code 2MM4) have been deposited in the Protein Data Bank (http://wwpdb.org/).

Assigned chemical shifts have been deposited at the Biological Magnetic Resonance Bank (BMRB) with ID 19845.