7XR2
3.1 Angstrom cryoEM icosahedral reconstruction of mud crab reovirus
Summary for 7XR2
| Entry DOI | 10.2210/pdb7xr2/pdb |
| EMDB information | 33403 |
| Descriptor | VP3, VP11, VP12 (3 entities in total) |
| Functional Keywords | reovirus, ds-rna virus, virus |
| Biological source | Scylla serrata reovirus SZ-2007 More |
| Total number of polymer chains | 17 |
| Total formula weight | 628042.69 |
| Authors | |
| Primary citation | Zhang, Q.,Gao, Y.,Baker, M.L.,Liu, S.,Jia, X.,Xu, H.,He, J.,Kaelber, J.T.,Weng, S.,Jiang, W. The structure of a 12-segmented dsRNA reovirus: New insights into capsid stabilization and organization. Plos Pathog., 19:e1011341-e1011341, 2023 Cited by PubMed Abstract: Infecting a wide range of hosts, members of Reovirales (formerly Reoviridae) consist of a genome with different numbers of segmented double stranded RNAs (dsRNA) encapsulated by a proteinaceous shell and carry out genome replication and transcription inside the virion. Several cryo-electron microscopy (cryo-EM) structures of reoviruses with 9, 10 or 11 segmented dsRNA genomes have revealed insights into genome arrangement and transcription. However, the structure and genome arrangement of 12-segmented Reovirales members remain poorly understood. Using cryo-EM, we determined the structure of mud crab reovirus (MCRV), a 12-segmented dsRNA virus that is a putative member of Reovirales in the non-turreted Sedoreoviridae family, to near-atomic resolutions with icosahedral symmetry (3.1 Å) and without imposing icosahedral symmetry (3.4 Å). These structures revealed the organization of the major capsid proteins in two layers: an outer T = 13 layer consisting of VP12 trimers and unique VP11 clamps, and an inner T = 1 layer consisting of VP3 dimers. Additionally, ten RNA dependent RNA polymerases (RdRp) were well resolved just below the VP3 layer but were offset from the 5-fold axes and arranged with D5 symmetry, which has not previously been seen in other members of Reovirales. The N-termini of VP3 were shown to adopt four unique conformations; two of which anchor the RdRps, while the other two conformations are likely involved in genome organization and capsid stability. Taken together, these structures provide a new level of understanding for capsid stabilization and genome organization of segmented dsRNA viruses. PubMed: 37083840DOI: 10.1371/journal.ppat.1011341 PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (3.1 Å) |
Structure validation
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