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

Background: Coronavirus envelope (CoV E) proteins have a predicted β-coil-β motif reported to target the Golgi complex. Results: This conserved domain forms β-structure on its own but is α-helical in the context of full-length SARS-CoV E protein. Conclusion: This domain is potentially involved in large conformational transitions. Significance: This is the first structural data of the extramembrane domain of any coronavirus E protein. 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.

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