1. Division of Structural Biology, The Wellcome Trust Centre for Human Genetics, University of Oxford, Roosevelt Drive, Headington, Oxford OX3 7BN, UK
2. Oxford Centre for Molecular Sciences, Central Chemistry Laboratory, University of Oxford, South Parks Road, Oxford OX1 3QT, UK
3. Institute of Biotechnology and Faculty of Biosciences, Viikki Biocenter, University of Helsinki, P.O. Box 56, Viikinkaari 5, 00014, Finland
4. The Wistar Institute, 3601 Spruce Street, Philadelphia, Pennsylvania 19104, USA
5. These authors contributed equally to this work
6. Present address: Biocomputing Unit, Centro Nacional de Biotecnología, Campus Universidad Autónoma, 28049 Madrid, Spain

Correspondence to: David I. Stuart^1,2Jaana K. H. Bamford³ Email: dave@strubi.ox.ac.uk
Email: jaana.bamford@helsinki.fi
Coordinates for proteins P3, P30, P31 and P16 within the icosahedral asymmetric unit have been deposited in the Protein Data Bank under accession code 1w8x.

Abstract

The structure of the membrane-containing bacteriophage PRD1 has been determined by X-ray crystallography at about 4 Å 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.

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