3IYL
Atomic CryoEM Structure of a Nonenveloped Virus Suggests How Membrane Penetration Protein is Primed for Cell Entry
Summary for 3IYL
| Entry DOI | 10.2210/pdb3iyl/pdb |
| EMDB information | 5160 |
| Descriptor | Outer capsid VP4, Core protein VP6, VP1, ... (5 entities in total) |
| Functional Keywords | non-enveloped virus, membrane penetration protein, autocleavage, myristol group, icosahedral virus, virus |
| Biological source | Grass carp reovirus More |
| Total number of polymer chains | 25 |
| Total formula weight | 1870350.56 |
| Authors | Zhang, X.,Jin, L.,Fang, Q.,Hui, W.,Zhou, Z.H. (deposition date: 2010-02-02, release date: 2010-05-12, Last modification date: 2024-11-20) |
| Primary citation | Zhang, X.,Jin, L.,Fang, Q.,Hui, W.H.,Zhou, Z.H. 3.3 A cryo-EM structure of a nonenveloped virus reveals a priming mechanism for cell entry. Cell(Cambridge,Mass.), 141:472-482, 2010 Cited by PubMed Abstract: To achieve cell entry, many nonenveloped viruses must transform from a dormant to a primed state. In contrast to the membrane fusion mechanism of enveloped viruses (e.g., influenza virus), this membrane penetration mechanism is poorly understood. Here, using single-particle cryo-electron microscopy, we report a 3.3 A structure of the primed, infectious subvirion particle of aquareovirus. The density map reveals side-chain densities of all types of amino acids (except glycine), enabling construction of a full-atom model of the viral particle. Our structure and biochemical results show that priming involves autocleavage of the membrane penetration protein and suggest that Lys84 and Glu76 may facilitate this autocleavage in a nucleophilic attack. We observe a myristoyl group, covalently linked to the N terminus of the penetration protein and embedded in a hydrophobic pocket. These results suggest a well-orchestrated process of nonenveloped virus entry involving autocleavage of the penetration protein prior to exposure of its membrane-insertion finger. PubMed: 20398923DOI: 10.1016/j.cell.2010.03.041 PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (3.3 Å) |
Structure validation
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