4N43
Human enterovirus 71 uncoating intermediate captured at atomic resolution
Summary for 4N43
| Entry DOI | 10.2210/pdb4n43/pdb |
| Descriptor | Capsid protein VP1, Capsid protein VP2, Capsid protein VP3 (3 entities in total) |
| Functional Keywords | hand-foot-and-mouth disease, picornavirus, human enterovirus 71, uncoating intermediate, icosahedral virus, pocket factor, virus |
| Biological source | Enterovirus A71 More |
| Cellular location | Host cytoplasmic vesicle membrane ; Peripheral membrane protein ; Cytoplasmic side . Virion : M9XM90 Q9WQJ0 Q9WPJ0 |
| Total number of polymer chains | 3 |
| Total formula weight | 86866.06 |
| Authors | |
| Primary citation | Lyu, K.,Ding, J.,Han, J.F.,Zhang, Y.,Wu, X.Y.,He, Y.L.,Qin, C.F.,Chen, R. Human enterovirus 71 uncoating captured at atomic resolution. J.Virol., 88:3114-3126, 2014 Cited by PubMed Abstract: Human enterovirus 71 (EV71) is the major causative agent of severe hand-foot-and-mouth diseases (HFMD) in young children, and structural characterization of EV71 during its life cycle can aid in the development of therapeutics against HFMD. Here, we present the atomic structures of the full virion and an uncoating intermediate of a clinical EV71 C4 strain to illustrate the structural changes in the full virion that lead to the formation of the uncoating intermediate prepared for RNA release. Although the VP1 N-terminal regions observed to penetrate through the junction channel at the quasi-3-fold axis in the uncoating intermediate of coxsackievirus A16 were not observed in the EV71 uncoating intermediate, drastic conformational changes occur in this region, as has been observed in all capsid proteins. Additionally, the RNA genome interacts with the N-terminal extensions of VP1 and residues 32 to 36 of VP3, both of which are situated at the bottom of the junction. These observations highlight the importance of the junction for genome release. Furthermore, EV71 uncoating is associated with apparent rearrangements and expansion around the 2- and 5-fold axes without obvious changes around the 3-fold axes. Therefore, these structures enabled the identification of hot spots for capsid rearrangements, which led to the hypothesis that the protomer interface near the junction and the 2-fold axis permits the opening of large channels for the exit of polypeptides and viral RNA, which is an uncoating mechanism that is likely conserved in enteroviruses. PubMed: 24352461DOI: 10.1128/JVI.03029-13 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (3.8011 Å) |
Structure validation
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