8XB8
The structure of ASFV A137R
Summary for 8XB8
| Entry DOI | 10.2210/pdb8xb8/pdb |
| EMDB information | 38214 |
| Descriptor | A137R (1 entity in total) |
| Functional Keywords | dodecahedron, african swine fever virus, polymer, viral protein |
| Biological source | African swine fever virus |
| Total number of polymer chains | 60 |
| Total formula weight | 966873.00 |
| Authors | |
| Primary citation | Li, C.,Jia, M.,Hao, T.,Peng, Q.,Peng, R.,Chai, Y.,Shi, Y.,Song, H.,Gao, G.F. African swine fever virus A137R assembles into a dodecahedron cage. J.Virol., 98:e0153623-e0153623, 2024 Cited by PubMed Abstract: African swine fever (ASF) is a highly contagious viral disease that affects domestic and wild pigs. The causative agent of ASF is African swine fever virus (ASFV), a large double-stranded DNA virus with a complex virion structure. Among the various proteins encoded by ASFV, A137R is a crucial structural protein associated with its virulence. However, the structure and molecular mechanisms underlying the functions of A137R remain largely unknown. In this study, we present the structure of A137R determined by cryogenic electron microscopy single-particle reconstruction, which reveals that A137R self-oligomerizes to form a dodecahedron-shaped cage composed of 60 polymers. The dodecahedron is literally equivalent to a 1 icosahedron where the icosahedral vertexes are located in the center of each dodecahedral facet. Within each facet, five A137R protomers are arranged in a head-to-tail orientation with a long N-terminal helix forming the edge through which adjacent facets stitch together to form the dodecahedral cage. Combining structural analysis and biochemical evidence, we demonstrate that the N-terminal domain of A137R is crucial and sufficient for mediating the assembly of the dodecahedron. These findings imply the role of A137R cage as a core component in the icosahedral ASFV virion and suggest a promising molecular scaffold for nanotechnology applications. PubMed: 38315014DOI: 10.1128/jvi.01536-23 PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (3.4 Å) |
Structure validation
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