3J23
The Enterovirus 71 empty capsid
Summary for 3J23
| Entry DOI | 10.2210/pdb3j23/pdb |
| Related | 3J22 |
| EMDB information | 5465 5466 |
| Descriptor | capsid protein VP1, capsid protein VP0, capsid protein VP3 (3 entities in total) |
| Functional Keywords | ev71, 80s, virus |
| Biological source | Human enterovirus 71 (EV71) More |
| Total number of polymer chains | 3 |
| Total formula weight | 77460.98 |
| Authors | Shingler, K.L. (deposition date: 2012-08-13, release date: 2013-04-03, Last modification date: 2024-02-21) |
| Primary citation | Shingler, K.L.,Yoder, J.L.,Carnegie, M.S.,Ashley, R.E.,Makhov, A.M.,Conway, J.F.,Hafenstein, S. The Enterovirus 71 A-particle Forms a Gateway to Allow Genome Release: A CryoEM Study of Picornavirus Uncoating. Plos Pathog., 9:e1003240-e1003240, 2013 Cited by PubMed Abstract: Since its discovery in 1969, enterovirus 71 (EV71) has emerged as a serious worldwide health threat. This human pathogen of the picornavirus family causes hand, foot, and mouth disease, and also has the capacity to invade the central nervous system to cause severe disease and death. Upon binding to a host receptor on the cell surface, the virus begins a two-step uncoating process, first forming an expanded, altered "A-particle", which is primed for genome release. In a second step after endocytosis, an unknown trigger leads to RNA expulsion, generating an intact, empty capsid. Cryo-electron microscopy reconstructions of these two capsid states provide insight into the mechanics of genome release. The EV71 A-particle capsid interacts with the genome near the icosahedral two-fold axis of symmetry, which opens to the external environment via a channel ∼10 Å in diameter that is lined with patches of negatively charged residues. After the EV71 genome has been released, the two-fold channel shrinks, though the overall capsid dimensions are conserved. These structural characteristics identify the two-fold channel as the site where a gateway forms and regulates the process of genome release. PubMed: 23555253DOI: 10.1371/journal.ppat.1003240 PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (9.2 Å) |
Structure validation
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