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Protein disk of tobacco mosaic virus at 2.8 Å resolution showing the interactions within and between subunits

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Abstract

Protein subunits in the two layers of the disk of tobacco mosaic virus have very similar conformations. Much of the bonding between subunits is polar, including salt-bridge systems. Arginine residues play a prominent part here and elsewhere. Interactions within each layer involve groups whose contacts can be adjusted to allow the transition from disk to virus helix. Aromatic clusters within each molecule are linked in a hydrophobic girdle encircling each ring.

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Author notes

  1. J. N. Champness

    Present address: Wellcome Research Laboratories, Langley Court, Beckenham, Kent, UK

Authors and Affiliations

  1. MRC Laboratory of Molecular Biology, Hills Road, Cambridge, UK

    A. C. Bloomer, J. N. Champness, G. Bricogne, R. Staden & A. Klug

Authors
  1. A. C. Bloomer
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  2. J. N. Champness
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  3. G. Bricogne
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  4. R. Staden
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  5. A. Klug
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Bloomer, A., Champness, J., Bricogne, G. et al. Protein disk of tobacco mosaic virus at 2.8 Å resolution showing the interactions within and between subunits. Nature 276, 362–368 (1978). https://doi.org/10.1038/276362a0

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