3FBZ
Crystal structure of ORF140 of the archaeal virus Acidianus Filamentous Virus 1 (AFV1)
Summary for 3FBZ
| Entry DOI | 10.2210/pdb3fbz/pdb |
| Descriptor | Putative uncharacterized protein, octyl beta-D-glucopyranoside, CHLORIDE ION, ... (4 entities in total) |
| Functional Keywords | archaeal virus, extremophiles, lipothrixviridae, structural protein |
| Biological source | Acidianus Filamentous Virus 1 |
| Total number of polymer chains | 4 |
| Total formula weight | 66195.03 |
| Authors | Goulet, A.,Prangishvili, D.,van Tilbeurgh, H.,Campanacci, V.,Cambillau, C. (deposition date: 2008-11-20, release date: 2009-11-10, Last modification date: 2024-11-20) |
| Primary citation | 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.USA, 106:21155-21160, 2009 Cited by PubMed Abstract: 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. PubMed: 19934032DOI: 10.1073/pnas.0909893106 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.3 Å) |
Structure validation
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