Loading
PDBj
MenuPDBj@FacebookPDBj@X(formerly Twitter)PDBj@BlueSkyPDBj@YouTubewwPDB FoundationwwPDBDonate
RCSB PDBPDBeBMRBAdv. SearchSearch help

6S2C

Acquired functional capsid structures in metazoan totivirus-like dsRNA virus.

Summary for 6S2C
Entry DOI10.2210/pdb6s2c/pdb
EMDB information10087
DescriptorCapsid protein (2 entities in total)
Functional Keywordsmosquito, totivirus, totiviridae, totivirus-like virus, dsrna, capsid, virus
Biological sourceOmono River virus
More
Total number of polymer chains2
Total formula weight182639.69
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 citationOkamoto, 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: 32413288
DOI: 10.1016/j.str.2020.04.016
PDB entries with the same primary citation
Experimental method
ELECTRON MICROSCOPY (3.2 Å)
Structure validation

237735

數據於2025-06-18公開中

PDB statisticsPDBj update infoContact PDBjnumon