| Autor: |
Goulet A; Architecture et Fonction des Macromolécules Biologiques, Centre national de la Recherche Scientifique and Universités Aix-Marseille I & II, Architecture et Fonction des Macromolécules Biologiques, Unité Mixte de Recherche 6098, Case 932, 163 avenue de Luminy, 13288 Marseille Cedex 9, France., Blangy S, Redder P, Prangishvili D, Felisberto-Rodrigues C, Forterre P, Campanacci V, Cambillau C |
| Jazyk: |
angličtina |
| Zdroj: |
Proceedings of the National Academy of Sciences of the United States of America [Proc Natl Acad Sci U S A] 2009 Dec 15; Vol. 106 (50), pp. 21155-60. Date of Electronic Publication: 2009 Nov 23. |
| DOI: |
10.1073/pnas.0909893106 |
| Abstrakt: |
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. |
| Databáze: |
MEDLINE |
| Externí odkaz: |
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