6S6L
Cryo-EM structure of murine norovirus (MNV-1)
Summary for 6S6L
| Entry DOI | 10.2210/pdb6s6l/pdb |
| EMDB information | 10103 |
| Descriptor | Capsid protein (1 entity in total) |
| Functional Keywords | norovirus, virus, capsid, vp1 |
| Biological source | Murine norovirus 1 |
| Total number of polymer chains | 3 |
| Total formula weight | 176101.79 |
| Authors | Snowden, J.S.,Hurdiss, D.L.,Adeyemi, O.O.,Ranson, N.A.,Herod, M.R.,Stonehouse, N.J. (deposition date: 2019-07-03, release date: 2020-05-13, Last modification date: 2025-07-02) |
| Primary citation | Snowden, J.S.,Hurdiss, D.L.,Adeyemi, O.O.,Ranson, N.A.,Herod, M.R.,Stonehouse, N.J. Dynamics in the murine norovirus capsid revealed by high-resolution cryo-EM. Plos Biol., 18:e3000649-e3000649, 2020 Cited by PubMed Abstract: Icosahedral viral capsids must undergo conformational rearrangements to coordinate essential processes during the viral life cycle. Capturing such conformational flexibility has been technically challenging yet could be key for developing rational therapeutic agents to combat infections. Noroviruses are nonenveloped, icosahedral viruses of global importance to human health. They are a common cause of acute gastroenteritis, yet no vaccines or specific antiviral agents are available. Here, we use genetics and cryo-electron microscopy (cryo-EM) to study the high-resolution solution structures of murine norovirus as a model for human viruses. By comparing our 3 structures (at 2.9- to 3.1-Å resolution), we show that whilst there is little change to the shell domain of the capsid, the radiating protruding domains are flexible, adopting distinct states both independently and synchronously. In doing so, the capsids sample a range of conformational space, with implications for maintaining virion stability and infectivity. PubMed: 32231352DOI: 10.1371/journal.pbio.3000649 PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (3.1 Å) |
Structure validation
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