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Comparisons of bacteriophage PRD1 and adenovirus protein structures and virion architectures have been instrumental in unraveling an evolutionary relationship and have led to a proposal of a phylogeny-based virus classification. The structure of the PRD1 spike protein P5 provides further insight into the evolution of viral proteins. The crystallized P5 fragment comprises two structural domains: a globular knob and a fibrous shaft. The head folds into a ten-stranded jelly roll beta barrel, which is structurally related to the tumor necrosis factor (TNF) and the PRD1 coat protein domains. The shaft domain is a structural counterpart to the adenovirus spike shaft. The structural relationships between PRD1, TNF, and adenovirus proteins suggest that the vertex proteins may have originated from an ancestral TNF-like jelly roll coat protein via a combination of gene duplication and deletion.

Original publication

DOI

10.1016/j.molcel.2005.03.019

Type

Journal article

Journal

Mol Cell

Publication Date

15/04/2005

Volume

18

Pages

161 - 170

Keywords

Adenoviruses, Human, Amino Acid Sequence, Bacteriophage PRD1, Capsid, Capsid Proteins, Crystallography, X-Ray, Evolution, Molecular, Models, Chemical, Models, Molecular, Molecular Sequence Data, Protein Structure, Tertiary, Sequence Homology, Amino Acid, Spectrum Analysis, Raman, Tumor Necrosis Factor-alpha, Viral Proteins