6v7b

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

spinqualitylabelsall models 6v7b, resolution 3.40Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 6v7b is a 48 chain structure with sequence from Pyrobaculum filamentous virus 1. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: Electron Microscopy, Resolution 3.4Å Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function CAPS1_PFV2 Self-assembles to form a helical, filamentous nucleocapsid mesuring 400 nm in length and 20 nm in width (Probable) (PubMed:32368353). Together with capsid protein 2, wraps arounds the DNA and maintains it in an A-form (Probable). Capsid proteins probably maintain the DNA in A-form by non-specific desolvation and specific coordination of the DNA phosphate groups by positively charged residues (Probable). This certainly protects the viral DNA under conditions such as the extreme desiccation of its host (Probable). CAPS1_PFV1 Publication Abstract from PubMed 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 A 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. Structure of a filamentous virus uncovers familial ties within the archaeal virosphere.,Wang F, Baquero DP, Su Z, Osinski T, Prangishvili D, Egelman EH, Krupovic M Virus Evol. 2020 Apr 29;6(1):veaa023. doi: 10.1093/ve/veaa023. eCollection 2020, Jan. PMID:32368353 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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