Summary for 6QCC
| Entry DOI | 10.2210/pdb6qcc/pdb |
| EMDB information | 4504 |
| Descriptor | Large coat-protein subunit, Small coat-protein subunit (2 entities in total) |
| Functional Keywords | comovirus capsid plant virus bbsv, virus |
| Biological source | Broad bean stain virus More |
| Total number of polymer chains | 2 |
| Total formula weight | 64837.64 |
| Authors | Lecorre, F.,Lai Jee Him, J.,Blanc, S.,Zeddam, J.-L.,Trapani, S.,Bron, P. (deposition date: 2018-12-27, release date: 2019-05-01, Last modification date: 2024-05-15) |
| Primary citation | Lecorre, F.,Lai-Kee-Him, J.,Blanc, S.,Zeddam, J.L.,Trapani, S.,Bron, P. The cryo-electron microscopy structure of Broad Bean Stain Virus suggests a common capsid assembly mechanism among comoviruses. Virology, 530:75-84, 2019 Cited by PubMed Abstract: The Broad bean stain virus (BBSV) is a member of the genus Comovirus infecting Fabaceae. The virus is transmitted through seed and by plant weevils causing severe and widespread disease worldwide. BBSV has a bipartite, positive-sense, single-stranded RNA genome encapsidated in icosahedral particles. We present here the cryo-electron microscopy reconstruction of the BBSV and an atomic model of the capsid proteins refined at 3.22 Å resolution. We identified residues involved in RNA/capsid interactions revealing a unique RNA genome organization. Inspection of the small coat protein C-terminal domain highlights a maturation cleavage between Leu567 and Leu568 and interactions of the C-terminal stretch with neighbouring small coat proteins within the capsid pentameric turrets. These interactions previously proposed to play a key role in the assembly of the Cowpea mosaic virus suggest a common capsid assembly mechanism throughout all comovirus species. PubMed: 30782565DOI: 10.1016/j.virol.2019.02.009 PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (3.22 Å) |
Structure validation
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