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| | <StructureSection load='6v7b' size='340' side='right'caption='[[6v7b]], [[Resolution|resolution]] 3.40Å' scene=''> | | <StructureSection load='6v7b' size='340' side='right'caption='[[6v7b]], [[Resolution|resolution]] 3.40Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[6v7b]] is a 48 chain structure with sequence from [http://en.wikipedia.org/wiki/Pyrobaculum_filamentous_virus_1 Pyrobaculum filamentous virus 1]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6V7B OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=6V7B FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[6v7b]] is a 48 chain structure with sequence from [https://en.wikipedia.org/wiki/Pyrobaculum_filamentous_virus_1 Pyrobaculum filamentous virus 1]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6V7B OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6V7B FirstGlance]. <br> |
| - | </td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=6v7b FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6v7b OCA], [http://pdbe.org/6v7b PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6v7b RCSB], [http://www.ebi.ac.uk/pdbsum/6v7b PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6v7b ProSAT]</span></td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Electron Microscopy, [[Resolution|Resolution]] 3.4Å</td></tr> |
| | + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=6v7b FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6v7b OCA], [https://pdbe.org/6v7b PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6v7b RCSB], [https://www.ebi.ac.uk/pdbsum/6v7b PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6v7b ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/CAPS1_PFV2 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).<ref>PMID:32368353</ref> <ref>PMID:32759221</ref> [https://www.uniprot.org/uniprot/CAPS1_PFV1 CAPS1_PFV1] |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| | [[Category: Pyrobaculum filamentous virus 1]] | | [[Category: Pyrobaculum filamentous virus 1]] |
| - | [[Category: Baquero, D P]] | + | [[Category: Baquero DP]] |
| - | [[Category: Egelman, E H]] | + | [[Category: Egelman EH]] |
| - | [[Category: Krupovic, M]] | + | [[Category: Krupovic M]] |
| - | [[Category: Prangishvili, D]] | + | [[Category: Prangishvili D]] |
| - | [[Category: Su, Z]] | + | [[Category: Su Z]] |
| - | [[Category: Wang, F]] | + | [[Category: Wang F]] |
| - | [[Category: Archaeal pilus]]
| + | |
| - | [[Category: Helical symmetry]]
| + | |
| - | [[Category: Structural protein]]
| + | |
| - | [[Category: Virus]]
| + | |
| Structural highlights
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).[1] [2] 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[3]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Wang F, Baquero DP, Su Z, Osinski T, Prangishvili D, Egelman EH, Krupovic M. Structure of a filamentous virus uncovers familial ties within the archaeal virosphere. Virus Evol. 2020 Apr 29;6(1):veaa023. doi: 10.1093/ve/veaa023. eCollection 2020, Jan. PMID:32368353 doi:http://dx.doi.org/10.1093/ve/veaa023
- ↑ Wang F, Baquero DP, Beltran LC, Su Z, Osinski T, Zheng W, Prangishvili D, Krupovic M, Egelman EH. Structures of filamentous viruses infecting hyperthermophilic archaea explain DNA stabilization in extreme environments. Proc Natl Acad Sci U S A. 2020 Aug 18;117(33):19643-19652. PMID:32759221 doi:10.1073/pnas.2011125117
- ↑ Wang F, Baquero DP, Su Z, Osinski T, Prangishvili D, Egelman EH, Krupovic M. Structure of a filamentous virus uncovers familial ties within the archaeal virosphere. Virus Evol. 2020 Apr 29;6(1):veaa023. doi: 10.1093/ve/veaa023. eCollection 2020, Jan. PMID:32368353 doi:http://dx.doi.org/10.1093/ve/veaa023
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