Loading
PDBj
MenuPDBj@FacebookPDBj@X(formerly Twitter)PDBj@BlueSkyPDBj@YouTubewwPDB FoundationwwPDB
RCSB PDBPDBeBMRBAdv. SearchSearch help

3FBL

Crystal structure of ORF132 of the archaeal virus Acidianus Filamentous Virus 1 (AFV1)

Summary for 3FBL
Entry DOI10.2210/pdb3fbl/pdb
DescriptorPutative uncharacterized protein, CHLORIDE ION (3 entities in total)
Functional Keywordsafv1, archaeal virus, extremophiles, lipothrixviridae, structural protein, dna-binding protein
Biological sourceAcidianus filamentous virus 1
Total number of polymer chains1
Total formula weight9204.05
Authors
Goulet, A.,Leulliot, N.,Prangishvili, D.,van Tilbeurgh, H.,Campanacci, V.,Cambillau, C. (deposition date: 2008-11-19, release date: 2009-11-10, Last modification date: 2023-12-27)
Primary citationGoulet, 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: 19934032
DOI: 10.1073/pnas.0909893106
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (1.95 Å)
Structure validation

227344

PDB entries from 2024-11-13

PDB statisticsPDBj update infoContact PDBjnumon