2MM4
Structure of a Conserved Golgi Complex-targeting Signal in Coronavirus Envelope Proteins
Summary for 2MM4
| Entry DOI | 10.2210/pdb2mm4/pdb |
| NMR Information | BMRB: 19845 |
| Descriptor | Envelope small membrane protein (1 entity in total) |
| Functional Keywords | sars coronavirus, envelope protein, membrane protein, viral protein |
| Biological source | SARS coronavirus (Human SARS coronavirus) |
| Total number of polymer chains | 1 |
| Total formula weight | 6313.60 |
| Authors | Li, Y.,Surya, W.,Claudine, S.,Torres, J. (deposition date: 2014-03-09, release date: 2014-04-02, Last modification date: 2024-05-15) |
| Primary citation | Li, Y.,Surya, W.,Claudine, S.,Torres, J. Structure of a conserved Golgi complex-targeting signal in coronavirus envelope proteins. J.Biol.Chem., 289:12535-12549, 2014 Cited by 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. PubMed: 24668816DOI: 10.1074/jbc.M114.560094 PDB entries with the same primary citation |
| Experimental method | SOLUTION NMR |
Structure validation
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