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| | <SX load='3j9x' size='340' side='right' viewer='molstar' caption='[[3j9x]], [[Resolution|resolution]] 3.80Å' scene=''> | | <SX load='3j9x' size='340' side='right' viewer='molstar' caption='[[3j9x]], [[Resolution|resolution]] 3.80Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[3j9x]] is a 60 chain structure with sequence from [http://en.wikipedia.org/wiki/Sulfolobus_islandicus_rod-shaped_virus_2 Sulfolobus islandicus rod-shaped virus 2]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3J9X OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3J9X FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[3j9x]] is a 60 chain structure with sequence from [https://en.wikipedia.org/wiki/Sulfolobus_islandicus_rod-shaped_virus_2 Sulfolobus islandicus rod-shaped virus 2]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3J9X OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3J9X FirstGlance]. <br> |
| - | </td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3j9x FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3j9x OCA], [http://pdbe.org/3j9x PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3j9x RCSB], [http://www.ebi.ac.uk/pdbsum/3j9x PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3j9x 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]] 3.8Å</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=3j9x FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3j9x OCA], [https://pdbe.org/3j9x PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3j9x RCSB], [https://www.ebi.ac.uk/pdbsum/3j9x PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3j9x ProSAT]</span></td></tr> |
| | </table> | | </table> |
| - | <div style="background-color:#fffaf0;">
| + | == Function == |
| - | == Publication Abstract from PubMed == | + | [https://www.uniprot.org/uniprot/CAPSD_SIRV2 CAPSD_SIRV2] Self-assembles to form a helical, filamentous nucleocapsid (PubMed:25999507). The capsid proteins wrap around the DNA and maintain it in an A-form by non-specific desolvation and specific coordination of the DNA phosphate groups by positively charged residues (Probable) (PubMed:25999507). This certainly protects the viral DNA under conditions such as the extreme desiccation of its host (Probable).<ref>PMID:25999507</ref> <ref>PMID:25999507</ref> <ref>PMID:32759221</ref> |
| - | Extremophiles, microorganisms thriving in extreme environmental conditions, must have proteins and nucleic acids that are stable at extremes of temperature and pH. The nonenveloped, rod-shaped virus SIRV2 (Sulfolobus islandicus rod-shaped virus 2) infects the hyperthermophilic acidophile Sulfolobus islandicus, which lives at 80 degrees C and pH 3. We have used cryo-electron microscopy to generate a three-dimensional reconstruction of the SIRV2 virion at ~4 angstrom resolution, which revealed a previously unknown form of virion organization. Although almost half of the capsid protein is unstructured in solution, this unstructured region folds in the virion into a single extended alpha helix that wraps around the DNA. The DNA is entirely in the A-form, which suggests a common mechanism with bacterial spores for protecting DNA in the most adverse environments.
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| - | Virology. A virus that infects a hyperthermophile encapsidates A-form DNA.,DiMaio F, Yu X, Rensen E, Krupovic M, Prangishvili D, Egelman EH Science. 2015 May 22;348(6237):914-7. doi: 10.1126/science.aaa4181. PMID:25999507<ref>PMID:25999507</ref>
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| - | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
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| - | </div> | + | |
| - | <div class="pdbe-citations 3j9x" style="background-color:#fffaf0;"></div> | + | |
| | | | |
| | ==See Also== | | ==See Also== |
| - | *[[Virus coat protein|Virus coat protein]] | + | *[[Virus coat proteins 3D structures|Virus coat proteins 3D structures]] |
| | == References == | | == References == |
| | <references/> | | <references/> |
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| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| | [[Category: Sulfolobus islandicus rod-shaped virus 2]] | | [[Category: Sulfolobus islandicus rod-shaped virus 2]] |
| - | [[Category: DiMaio, F]] | + | [[Category: DiMaio F]] |
| - | [[Category: Egelman, E]] | + | [[Category: Egelman E]] |
| - | [[Category: Krupovic, M]] | + | [[Category: Krupovic M]] |
| - | [[Category: Prangishvili, D]] | + | [[Category: Prangishvili D]] |
| - | [[Category: Rensen, E]] | + | [[Category: Rensen E]] |
| - | [[Category: Yu, X]] | + | [[Category: Yu X]] |
| - | [[Category: Archaeal virus]]
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| - | [[Category: Helical symmetry]]
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| - | [[Category: Virus]]
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| Structural highlights
Function
CAPSD_SIRV2 Self-assembles to form a helical, filamentous nucleocapsid (PubMed:25999507). The capsid proteins wrap around the DNA and maintain it in an A-form by non-specific desolvation and specific coordination of the DNA phosphate groups by positively charged residues (Probable) (PubMed:25999507). This certainly protects the viral DNA under conditions such as the extreme desiccation of its host (Probable).[1] [2] [3]
See Also
References
- ↑ DiMaio F, Yu X, Rensen E, Krupovic M, Prangishvili D, Egelman EH. Virology. A virus that infects a hyperthermophile encapsidates A-form DNA. Science. 2015 May 22;348(6237):914-7. doi: 10.1126/science.aaa4181. PMID:25999507 doi:http://dx.doi.org/10.1126/science.aaa4181
- ↑ DiMaio F, Yu X, Rensen E, Krupovic M, Prangishvili D, Egelman EH. Virology. A virus that infects a hyperthermophile encapsidates A-form DNA. Science. 2015 May 22;348(6237):914-7. doi: 10.1126/science.aaa4181. PMID:25999507 doi:http://dx.doi.org/10.1126/science.aaa4181
- ↑ 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
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