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

Orlova, Elena V.; Dube, Prakash; Beckmann, Erich; Zemlin, Friedrich; Lurz, Rudi; Trautner, Thomas A.; Tavares, Paulo

doi:10.1038/12303

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

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Beckmann, Erich
Inorganic Chemistry, Fritz Haber Institute, Max Planck Society;

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Zemlin, Friedrich
Inorganic Chemistry, Fritz Haber Institute, Max Planck Society;

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Citation

Orlova, E. V., Dube, P., Beckmann, E., Zemlin, F., Lurz, R., Trautner, T. A., et al. (1999). Structure of the 13-fold symmetric portal protein of bacteriophage SPP1. Nature Structural and Molecular Biology, 6(9), 842-846. doi:10.1038/12303.

Cite as: https://hdl.handle.net/21.11116/0000-0006-5B8F-4

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.