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Insights into assembly from structural analysis of bacteriophage PRD1

Nature volume 432, pages 68–74 (2004)Cite this article

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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Figure 1: Architecture and structural components of bacteriophage PRD1.
Figure 2: Switching of the P3 termini.
Figure 3: Vertex organization.

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Acknowledgements

We thank M.-L. Perälä and S. Ollila for technical assistance, the staff at the European Synchrotron Radiation Facility for beamline support, and E. Mancini for assistance with data collection. This investigation was supported by research grants from the Academy of Finland to J.K.H.B. and S.J.B., research grants and the Finnish Centre of Excellence Program (2000–2005) from the Academy of Finland to D.H.B., a grant from the National Science Foundation to R.M.B., the Biotechnology and Biological Sciences Research Council and the Medical Research Council, UK and a grant from the Human Frontiers Science Program to D.I.S., R.M.B. and D.H.B. S.D.F. is supported by the Wellcome Trust, J.M.G. by the Royal Society and D.I.S. by the UK Medical Research Council.

Author information

Author notes

  1. Carmen San Martín

    Present address: Biocomputing Unit, Centro Nacional de Biotecnología, Campus Universidad Autónoma, 28049, Madrid, Spain

  2. Nicola G. A. Abrescia and Joseph J. B. Cockburn: These authors contributed equally to this work

Authors and Affiliations

  1. Division of Structural Biology, The Wellcome Trust Centre for Human Genetics, University of Oxford, Roosevelt Drive, Headington, OX3 7BN, Oxford, UK

    Nicola G. A. Abrescia, Joseph J. B. Cockburn, Jonathan M. Grimes, Geoffrey C. Sutton, Jonathan M. Diprose, Stephen D. Fuller & David I. Stuart

  2. Oxford Centre for Molecular Sciences, Central Chemistry Laboratory, University of Oxford, South Parks Road, OX1 3QT, Oxford, UK

    Joseph J. B. Cockburn & David I. Stuart

  3. Institute of Biotechnology and Faculty of Biosciences, Viikki Biocenter, University of Helsinki, P.O. Box 56, Viikinkaari 5, 00014, Finland

    Sarah J. Butcher, Dennis H. Bamford & Jaana K. H. Bamford

  4. The Wistar Institute, 3601 Spruce Street, Philadelphia, Pennsylvania, 19104, USA

    Carmen San Martín & Roger M. Burnett

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Correspondence to David I. Stuart or Jaana K. H. Bamford.

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Supplementary information

Supplementary Figure

Curves of data completeness and correlation coefficient versus resolution for cell1 and cell2 data. (DOC 416 kb)

Supplementary Methods

Describes the calculation of packing density in the cavity under the vertex. (DOC 24 kb)

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Abrescia, N., Cockburn, J., Grimes, J. et al. Insights into assembly from structural analysis of bacteriophage PRD1. Nature 432, 68–74 (2004). https://doi.org/10.1038/nature03056

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