6S2C
Acquired functional capsid structures in metazoan totivirus-like dsRNA virus.
Summary for 6S2C
Entry DOI | 10.2210/pdb6s2c/pdb |
EMDB information | 10087 |
Descriptor | Capsid protein (2 entities in total) |
Functional Keywords | mosquito, totivirus, totiviridae, totivirus-like virus, dsrna, capsid, virus |
Biological source | Omono River virus More |
Total number of polymer chains | 2 |
Total formula weight | 182639.69 |
Authors | Okamoto, K.,Larsson, S.D.D.,Maia, R.N.C.F.,Murata, K.,Hajdu, J.,Iwasaki, K.,Miyazaki, N. (deposition date: 2019-06-20, release date: 2020-04-29, Last modification date: 2024-05-22) |
Primary citation | Okamoto, K.,Ferreira, R.J.,Larsson, D.S.D.,Maia, F.R.N.C.,Isawa, H.,Sawabe, K.,Murata, K.,Hajdu, J.,Iwasaki, K.,Kasson, P.M.,Miyazaki, N. Acquired Functional Capsid Structures in Metazoan Totivirus-like dsRNA Virus. Structure, 28:888-896.e3, 2020 Cited by PubMed Abstract: Non-enveloped icosahedral double-stranded RNA (dsRNA) viruses possess multifunctional capsids required for their proliferation. Whereas protozoan/fungal dsRNA viruses have a relatively simple capsid structure, which suffices for the intracellular phase in their life cycle, metazoan dsRNA viruses have acquired additional structural features as an adaptation for extracellular cell-to-cell transmission in multicellular hosts. Here, we present the first atomic model of a metazoan dsRNA totivirus-like virus and the structure reveals three unique structural traits: a C-terminal interlocking arm, surface projecting loops, and an obstruction at the pore on the 5-fold symmetry axis. These traits are keys to understanding the capsid functions of metazoan dsRNA viruses, such as particle stability and formation, cell entry, and endogenous intraparticle transcription of mRNA. On the basis of molecular dynamics simulations of the obstructed pore, we propose a possible mechanism of intraparticle transcription in totivirus-like viruses, which dynamically switches between open and closed states of the pore(s). PubMed: 32413288DOI: 10.1016/j.str.2020.04.016 PDB entries with the same primary citation |
Experimental method | ELECTRON MICROSCOPY (3.2 Å) |
Structure validation
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