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Recent, primarily structural observations indicate that related viruses, harboring no sequence similarity, infect hosts of different domains of life. One such clade of viruses, defined by common capsid architecture and coat protein fold, is the so-called PRD1-adenovirus lineage. Here we report the structure of the marine lipid-containing bacteriophage PM2 determined by crystallographic analyses of the entire approximately 45 MDa virion and of the outer coat proteins P1 and P2, revealing PM2 to be a primeval member of the PRD1-adenovirus lineage with an icosahedral shell and canonical double beta barrel major coat protein. The view of the lipid bilayer, richly decorated with membrane proteins, constitutes a rare visualization of an in vivo membrane. The viral membrane proteins P3 and P6 are organized into a lattice, suggesting a possible assembly pathway to produce the mature virus.

Original publication

DOI

10.1016/j.molcel.2008.06.026

Type

Journal article

Journal

Mol Cell

Publication Date

05/09/2008

Volume

31

Pages

749 - 761

Keywords

Biological Evolution, Calcium, Capsid Proteins, Corticoviridae, Crystallography, X-Ray, Lipids, Models, Molecular, Molecular Sequence Data, Protein Conformation, Virion, Viruses