PMID:15525981
| Citation |
Abrescia, NG, Cockburn, JJ, Grimes, JM, Sutton, GC, Diprose, JM, Butcher, SJ, Fuller, SD, San Martín, C, Burnett, RM, Stuart, DI, Bamford, DH and Bamford, JK (2004) Insights into assembly from structural analysis of bacteriophage PRD1. Nature 432:68-74 |
|---|---|
| Abstract |
The structure of the membrane-containing bacteriophage PRD1 has been determined by X-ray crystallography at about 4 A resolution. Here we describe the structure and location of proteins P3, P16, P30 and P31. Different structural proteins seem to have specialist roles in controlling virus assembly. The linearly extended P30 appears to nucleate the formation of the icosahedral facets (composed of trimers of the major capsid protein, P3) and acts as a molecular tape-measure, defining the size of the virus and cementing the facets together. Pentamers of P31 form the vertex base, interlocking with subunits of P3 and interacting with the membrane protein P16. The architectural similarities with adenovirus and one of the largest known virus particles PBCV-1 support the notion that the mechanism of assembly of PRD1 is scaleable and applies across the major viral lineage formed by these viruses. |
| Links |
PubMed Online version:10.1038/nature03056 |
| Keywords |
Amino Acid Sequence; Bacteriophage PRD1/chemistry; Bacteriophage PRD1/ultrastructure; Capsid/chemistry; Capsid/ultrastructure; Cryoelectron Microscopy; Crystallography, X-Ray; Models, Molecular; Molecular Sequence Data; Protein Structure, Quaternary; Protein Subunits/chemistry; Viral Structural Proteins/chemistry; Viral Structural Proteins/ultrastructure; Virion/chemistry; Virion/ultrastructure; Virus Assembly |
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