6S2C

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


Experimental Data Snapshot

  • Method: ELECTRON MICROSCOPY
  • Resolution: 3.20 Å
  • Aggregation State: PARTICLE 
  • Reconstruction Method: SINGLE PARTICLE 

wwPDB Validation   3D Report Full Report


This is version 1.2 of the entry. See complete history


Literature

Acquired Functional Capsid Structures in Metazoan Totivirus-like dsRNA Virus.

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.

(2020) Structure 28: 888-896.e3

  • DOI: https://doi.org/10.1016/j.str.2020.04.016
  • Primary Citation of Related Structures:  
    6S2C

  • 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).


  • Organizational Affiliation

    Program in Molecular Biophysics, Department of Cell and Molecular Biology, Uppsala University, Uppsala, Sweden. Electronic address: kenta.okamoto@icm.uu.se.


Macromolecules
Find similar proteins by:  (by identity cutoff)  |  3D Structure
Entity ID: 1
MoleculeChains Sequence LengthOrganismDetailsImage
Capsid protein840Omono River virusMutation(s): 0 
UniProt
Find proteins for E1CI69 (Omono River virus)
Explore E1CI69 
Go to UniProtKB:  E1CI69
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupE1CI69
Sequence Annotations
Expand
  • Reference Sequence
Find similar proteins by:  (by identity cutoff)  |  3D Structure
Entity ID: 2
MoleculeChains Sequence LengthOrganismDetailsImage
Capsid protein842Omono River virusMutation(s): 0 
UniProt
Find proteins for E1CI69 (Omono River virus)
Explore E1CI69 
Go to UniProtKB:  E1CI69
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupE1CI69
Sequence Annotations
Expand
  • Reference Sequence
Experimental Data & Validation

Experimental Data

  • Method: ELECTRON MICROSCOPY
  • Resolution: 3.20 Å
  • Aggregation State: PARTICLE 
  • Reconstruction Method: SINGLE PARTICLE 
EM Software:
TaskSoftware PackageVersion
RECONSTRUCTIONRELION2.1
RECONSTRUCTIONjspr
MODEL REFINEMENTPHENIX1.11.1

Structure Validation

View Full Validation Report



Entry History & Funding Information

Deposition Data


Funding OrganizationLocationGrant Number
Swedish Research CouncilSweden2018-03387
Swedish Research CouncilSweden2018-00421
Swedish Research CouncilSwedenJA2014-5721

Revision History  (Full details and data files)

  • Version 1.0: 2020-04-29
    Type: Initial release
  • Version 1.1: 2020-05-27
    Changes: Database references
  • Version 1.2: 2020-08-19
    Changes: Database references