7ANM
Nudaurelia capensis omega virus capsid: virus-like particles expressed in Nicotiana benthamiana
This is a non-PDB format compatible entry.
Summary for 7ANM
| Entry DOI | 10.2210/pdb7anm/pdb |
| EMDB information | 11830 |
| Descriptor | p70 (2 entities in total) |
| Functional Keywords | icosahedral virus, auto-catalytic cleavage, virus maturation, transient expression, virus like particle |
| Biological source | Nudaurelia capensis omega virus More |
| Total number of polymer chains | 8 |
| Total formula weight | 279639.72 |
| Authors | Castells-Graells, R.,Ribeiro, J.R.S.,Domitrovic, T.,Hesketh, E.L.,Scarff, C.A.,Johnson, J.E.,Ranson, N.A.,Lawson, D.M.,Lomonossoff, G.P. (deposition date: 2020-10-12, release date: 2021-08-25, Last modification date: 2024-07-10) |
| Primary citation | Castells-Graells, R.,Ribeiro, J.R.S.,Domitrovic, T.,Hesketh, E.L.,Scarff, C.A.,Johnson, J.E.,Ranson, N.A.,Lawson, D.M.,Lomonossoff, G.P. Plant-expressed virus-like particles reveal the intricate maturation process of a eukaryotic virus. Commun Biol, 4:619-619, 2021 Cited by PubMed Abstract: Many virus capsids undergo exquisitely choreographed maturation processes in their host cells to produce infectious virions, and these remain poorly understood. As a tool for studying virus maturation, we transiently expressed the capsid protein of the insect virus Nudaurelia capensis omega virus (NωV) in Nicotiana benthamiana and were able to purify both immature procapsids and mature capsids from infiltrated leaves by varying the expression time. Cryo-EM analysis of the plant-produced procapsids and mature capsids to 6.6 Å and 2.7 Å resolution, respectively, reveals that in addition to large scale rigid body motions, internal regions of the subunits are extensively remodelled during maturation, creating the active site required for autocatalytic cleavage and infectivity. The mature particles are biologically active in terms of their ability to lyse membranes and have a structure that is essentially identical to authentic virus. The ability to faithfully recapitulate and visualize a complex maturation process in plants, including the autocatalytic cleavage of the capsid protein, has revealed a ~30 Å translation-rotation of the subunits during maturation as well as conformational rearrangements in the N and C-terminal helical regions of each subunit. PubMed: 34031522DOI: 10.1038/s42003-021-02134-w PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (2.72 Å) |
Structure validation
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