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Tetrameric coiled coil domain of Sendai virus phosphoprotein

Nature Structural Biology volume 7, pages 777–781 (2000)Cite this article

Abstract

The high resolution X-ray structure of the Sendai virus oligomerization domain reveals a homotetrameric coiled coil structure with many details that are different from classic coiled coils with canonical hydrophobic heptad repeats. Alternatives to the classic knobs-into-holes packing lead to differences in supercoil pitch and diameter that allow water molecules inside the core. This open and more hydrophilic structure does not seem to be destabilized by mutations that would be expected to disrupt classic coiled coils.

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Figure 1: Structure of the oligomerization domain of P protein.
Figure 2: Layers in the core of the coiled coil.
Figure 3: Sequence and geometry of the oligomerization domain.
Figure 4: Implications of the structure for the interactions with other proteins.

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Acknowledgements

We thank J.-B. Marq (CMU, Geneva) for technical assistance, D. Kolakofsky (CMU, Geneva) for discussions and support and W. Weissenhorn (EMBL, Grenoble) for critical comments on the text.

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Authors and Affiliations

  1. European Synchrotron Radiation Facility, Grenoble cedex, France

    Nicolas Tarbouriech & Wilhelm P. Burmeister

  2. Department of Genetics and Microbiology, University of Geneva Medical School, CMU, 9 avenue de Champel, Geneva, 4, CH-1211, Switzerland

    Joseph Curran

  3. European Molecular Biology Laboratory, Grenoble outstation, c/o ILL, BP 156, Grenoble, cedex 9, F-38042, France

    Rob W.H. Ruigrok

  4. Forschungszentrum Jülich, BP 220, Grenoble cedex, F-38043, France

    Wilhelm P. Burmeister

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  1. Nicolas Tarbouriech
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Correspondence to Wilhelm P. Burmeister.

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Tarbouriech, N., Curran, J., Ruigrok, R. et al. Tetrameric coiled coil domain of Sendai virus phosphoprotein. Nat Struct Mol Biol 7, 777–781 (2000). https://doi.org/10.1038/79013

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