6V7B

Cryo-EM reconstruction of Pyrobaculum filamentous virus 2 (PFV2)

Summary for 6V7B

• Entry DOI: 10.2210/pdb6v7b/pdb
• EMDB information: 21094
• Descriptor: A-DNA, Structural protein VP1, Structural protein VP2, ... (4 entities in total)
• Functional Keywords: helical symmetry, archaeal pilus, structural protein, virus
• Biological source: Pyrobaculum filamentous virus 1; More
• Total number of polymer chains: 48
• Total formula weight: 896528.49

Authors

Wang, F.,Baquero, D.P.,Su, Z.,Prangishvili, D.,Krupovic, M.,Egelman, E.H. (deposition date: 2019-12-08, release date: 2020-04-01, Last modification date: 2024-10-09)

Primary citation

Wang, F.,Baquero, D.P.,Su, Z.,Osinski, T.,Prangishvili, D.,Egelman, E.H.,Krupovic, M.
Structure of a filamentous virus uncovers familial ties within the archaeal virosphere.
Virus Evol, 6:veaa023-veaa023, 2020

PubMed Abstract: Viruses infecting hyperthermophilic archaea represent one of the most enigmatic parts of the global virome, with viruses from different families showing no genomic relatedness to each other or to viruses of bacteria and eukaryotes. Tristromaviruses, which build enveloped filamentous virions and infect hyperthermophilic neutrophiles of the order Thermoproteales, represent one such enigmatic virus families. They do not share genes with viruses from other families and have been believed to represent an evolutionarily independent virus lineage. A cryo-electron microscopic reconstruction of the tristromavirus Pyrobaculum filamentous virus 2 at 3.4 Å resolution shows that the virion is constructed from two paralogous major capsid proteins (MCP) which transform the linear dsDNA genome of the virus into A-form by tightly wrapping around it. Unexpectedly, the two MCP are homologous to the capsid proteins of other filamentous archaeal viruses, uncovering a deep evolutionary relationship within the archaeal virosphere.

PubMed: 32368353
DOI: 10.1093/ve/veaa023

Experimental method

ELECTRON MICROSCOPY (3.4 Å)