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Crystal structure of ORF140 of the archaeal virus Acidianus Filamentous Virus 1 (AFV1)
Structural highlights
FunctionCAPS1_AFV1Y Self-assembles to form a helical, filamentous nucleocapsid mesuring 900 nm in length and 24 nm in width (Probable) (PubMed:19934032). Together with capsid protein 2, 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 PubMedAcidianus 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
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