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Structure of the 13-fold symmetric portal protein of bacteriophage SPP1

Nature Structural Biology volume 6, pages 842–846 (1999)Cite this article

Abstract

We have determined the three-dimensional structure of bacteriophage SPP1 portal protein (gp6) using electron microscopy at liquid-helium temperatures and angular reconstitution. The 13-fold symmetric gp6 oligomer is a turbine-shaped structure with three distinct regions: a conical stem with a central channel; the turbine wings region; and a fringe of small 'tentacles' at the end of the channel exposed to the viral head interior. The tentacle region appears flexible and may be associated with a particular function — sensing when the correct amount of DNA has been packaged. The three-dimensional structure of the gp6 SizA mutant, which packages a smaller chromosome, reveals significant differences in that region.

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Figure 1: Three-dimensional reconstruction procedures.
Figure 2: The structure of SPP1 wild type portal protein at 18 Å resolution.
Figure 3: SPP1 wild type portal protein versus the SizA packaging mutant.

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Acknowledgements

We are indebted to A. Isidro (ITQB, Oeiras) for communicating results prior to publication, and to R. Schmidt and M. Schatz for help with the IMAGIC image processing software. This work was supported in part by the Deutsche Forschungsgemeinschaft, and also by the EC.

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Author notes

  1. Prakash Dube

    Present address: Institut für Molekularbiologie und Tumorforschung, Emil-Mannkopff. Str. 2, D-35037, Marburg, Germany

  2. Paulo Tavares

    Present address: Unité de Pathogénie Microbienne Moléculaire and Unité INSERM U389, Institut Pasteur, Rue du Dr. Roux 28, F-75724, Paris, Cédéx 15, France

Authors and Affiliations

  1. Department of Biochemistry, Imperial College of Science, Technology and Medicine, Wolfson Laboratories, London, SW7 2AY, UK

    Elena V. Orlova, Prakash Dube & Marin van Heel

  2. Fritz-Haber-Institut der Max-Planck-Gesellschaft, Faradayweg 4-6, Berlin, D-14195, Germany

    Prakash Dube, Erich Beckmann & Friedrich Zemlin

  3. Max-Planck-Institut für Molekulare Genetik, Ihnestrabe 73, Berlin, D-14195, Germany

    Rudi Lurz, Thomas A. Trautner & Paulo Tavares

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Correspondence to Marin van Heel.

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Orlova, E., Dube, P., Beckmann, E. et al. Structure of the 13-fold symmetric portal protein of bacteriophage SPP1 . Nat Struct Mol Biol 6, 842–846 (1999). https://doi.org/10.1038/12303

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