|
|
| Line 3: |
Line 3: |
| | <StructureSection load='3fbl' size='340' side='right'caption='[[3fbl]], [[Resolution|resolution]] 1.95Å' scene=''> | | <StructureSection load='3fbl' size='340' side='right'caption='[[3fbl]], [[Resolution|resolution]] 1.95Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[3fbl]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Afv-1 Afv-1]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3FBL OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3FBL FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[3fbl]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Acidianus_filamentous_virus_1 Acidianus filamentous virus 1]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3FBL OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3FBL FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene></td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.95Å</td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">AFV1_ORF132 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=235266 AFV-1])</td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene></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=3fbl FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3fbl OCA], [https://pdbe.org/3fbl PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3fbl RCSB], [https://www.ebi.ac.uk/pdbsum/3fbl PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3fbl ProSAT]</span></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=3fbl FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3fbl OCA], [https://pdbe.org/3fbl PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3fbl RCSB], [https://www.ebi.ac.uk/pdbsum/3fbl PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3fbl ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/CAPS2_AFV1Y CAPS2_AFV1Y] Self-assembles to form a helical, filamentous nucleocapsid mesuring 900 nm in length and 24 nm in width (PubMed:19934032) (Probable). Together with capsid protein 1, 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:19934032</ref> <ref>PMID:32759221</ref> |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
| Line 21: |
Line 23: |
| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Afv-1]] | + | [[Category: Acidianus filamentous virus 1]] |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Cambillau, C]] | + | [[Category: Cambillau C]] |
| - | [[Category: Campanacci, V]] | + | [[Category: Campanacci V]] |
| - | [[Category: Goulet, A]] | + | [[Category: Goulet A]] |
| - | [[Category: Leulliot, N]] | + | [[Category: Leulliot N]] |
| - | [[Category: Prangishvili, D]] | + | [[Category: Prangishvili D]] |
| - | [[Category: Tilbeurgh, H van]] | + | [[Category: Van Tilbeurgh H]] |
| - | [[Category: Afv1]]
| + | |
| - | [[Category: Archaeal virus]]
| + | |
| - | [[Category: Dna-binding protein]]
| + | |
| - | [[Category: Extremophile]]
| + | |
| - | [[Category: Lipothrixviridae]]
| + | |
| - | [[Category: Structural protein]]
| + | |
| Structural highlights
Function
CAPS2_AFV1Y Self-assembles to form a helical, filamentous nucleocapsid mesuring 900 nm in length and 24 nm in width (PubMed:19934032) (Probable). Together with capsid protein 1, 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]
Publication Abstract from PubMed
Acidianus filamentous virus 1 (AFV1), a member of the Lipothrixviridae family, infects the hyperthermophilic, acidophilic crenarchaeaon Acidianus hospitalis. The virion, covered with a lipidic outer shell, is 9,100-A long and contains a 20.8-kb linear dsDNA genome. We have identified the two major coat proteins of the virion (MCPs; 132 and 140 amino acids). They bind DNA and form filaments when incubated with linear dsDNA. A C-terminal domain is identified in their crystal structure with a four-helix-bundle fold. In the topological model of the virion filament core, the genomic dsDNA superhelix wraps around the AFV1-132 basic protein, and the AFV1-140 basic N terminus binds genomic DNA, while its lipophilic C-terminal domain is imbedded in the lipidic outer shell. The four-helix bundle fold of the MCPs from AFV1 is identical to that of the coat protein (CP) of Sulfolobus islandicus rod-shaped virus (SIRV), a member of the Rudiviridae family. Despite low sequence identity between these proteins, their high degree of structural similarity suggests that they could have derived from a common ancestor and could thus define an yet undescribed viral lineage.
Acidianus filamentous virus 1 coat proteins display a helical fold spanning the filamentous archaeal viruses lineage.,Goulet A, Blangy S, Redder P, Prangishvili D, Felisberto-Rodrigues C, Forterre P, Campanacci V, Cambillau C Proc Natl Acad Sci U S A. 2009 Dec 15;106(50):21155-60. Epub 2009 Nov 23. PMID:19934032[3]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Goulet A, Blangy S, Redder P, Prangishvili D, Felisberto-Rodrigues C, Forterre P, Campanacci V, Cambillau C. Acidianus filamentous virus 1 coat proteins display a helical fold spanning the filamentous archaeal viruses lineage. Proc Natl Acad Sci U S A. 2009 Dec 15;106(50):21155-60. Epub 2009 Nov 23. PMID:19934032
- ↑ 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
- ↑ Goulet A, Blangy S, Redder P, Prangishvili D, Felisberto-Rodrigues C, Forterre P, Campanacci V, Cambillau C. Acidianus filamentous virus 1 coat proteins display a helical fold spanning the filamentous archaeal viruses lineage. Proc Natl Acad Sci U S A. 2009 Dec 15;106(50):21155-60. Epub 2009 Nov 23. PMID:19934032
|
