5X29
NMR structure of the SARS Coronavirus E protein pentameric ion channel
Summary for 5X29
| Entry DOI | 10.2210/pdb5x29/pdb |
| Related | 2MM4 |
| NMR Information | BMRB: 36049 |
| Descriptor | Envelope small membrane protein (1 entity in total) |
| Functional Keywords | membrane protein, viral protein, envelope protein, ion channel, pentamer |
| Biological source | Human SARS coronavirus (SARS-CoV) |
| Total number of polymer chains | 5 |
| Total formula weight | 45017.70 |
| Authors | Torres, J.,Surya, W.,Li, Y. (deposition date: 2017-01-31, release date: 2017-06-07, Last modification date: 2024-05-15) |
| Primary citation | Surya, W.,Li, Y.,Torres, J. Structural model of the SARS coronavirus E channel in LMPG micelles Biochim. Biophys. Acta, 1860:1309-1317, 2018 Cited by PubMed Abstract: Coronaviruses (CoV) cause common colds in humans, but are also responsible for the recent Severe Acute, and Middle East, respiratory syndromes (SARS and MERS, respectively). A promising approach for prevention are live attenuated vaccines (LAVs), some of which target the envelope (E) protein, which is a small membrane protein that forms ion channels. Unfortunately, detailed structural information is still limited for SARS-CoV E, and non-existent for other CoV E proteins. Herein, we report a structural model of a SARS-CoV E construct in LMPG micelles with, for the first time, unequivocal intermolecular NOEs. The model corresponding to the detergent-embedded region is consistent with previously obtained orientational restraints obtained in lipid bilayers and in vivo escape mutants. The C-terminal domain is mostly α-helical, and extramembrane intermolecular NOEs suggest interactions that may affect the TM channel conformation. PubMed: 29474890DOI: 10.1016/j.bbamem.2018.02.017 PDB entries with the same primary citation |
| Experimental method | SOLUTION NMR |
Structure validation
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