2MM4

Structure of a conserved Golgi complex-targeting signal in coronavirus envelope proteins.

(2014) J Biol Chem 289: 12535-12549

• PubMed: 24668816 Search on PubMedSearch on PubMed Central
• DOI: https://doi.org/10.1074/jbc.M114.560094
• Primary Citation of Related Structures:  
  2MM4


• PubMed Abstract: 
  

  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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Organizational Affiliation: 

From the School of Biological Sciences, Nanyang Technological University, 60 Nanyang Drive, 637551 Singapore.