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| == Function == | | == Function == |
| [https://www.uniprot.org/uniprot/CAPSD_SPTNK CAPSD_SPTNK] | | [https://www.uniprot.org/uniprot/CAPSD_SPTNK CAPSD_SPTNK] |
| <div style="background-color:#fffaf0;">
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| == Publication Abstract from PubMed ==
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| "Sputnik" is a dsDNA virus, referred to as a virophage, that is coassembled with Mimivirus in the host amoeba. We have used cryo-EM to produce an electron density map of the icosahedral Sputnik virus at 3.5-A resolution, sufficient to verify the identity of most amino acids in the capsid proteins and to establish the identity of the pentameric protein forming the fivefold vertices. It was also shown that the virus lacks an internal membrane. The capsid is organized into a T = 27 lattice in which there are 260 trimeric capsomers and 12 pentameric capsomers. The trimeric capsomers consist of three double "jelly-roll" major capsid proteins creating pseudohexameric capsomer symmetry. The pentameric capsomers consist of five single jelly-roll proteins. The release of the genome by displacing one or more of the pentameric capsomers may be the result of a low-pH environment. These results suggest a mechanism of Sputnik DNA ejection that probably also occurs in other big icosahedral double jelly-roll viruses such as Adenovirus. In this study, the near-atomic resolution structure of a virus has been established where crystallization for X-ray crystallography was not feasible.
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| Structure of Sputnik, a virophage, at 3.5-A resolution.,Zhang X, Sun S, Xiang Y, Wong J, Klose T, Raoult D, Rossmann MG Proc Natl Acad Sci U S A. 2012 Nov 6;109(45):18431-6. doi:, 10.1073/pnas.1211702109. Epub 2012 Oct 22. PMID:23091035<ref>PMID:23091035</ref>
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| From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
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| </div>
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| <div class="pdbe-citations 3j26" style="background-color:#fffaf0;"></div>
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| == References ==
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| <references/>
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| __TOC__ | | __TOC__ |
| </SX> | | </SX> |
