Skip to main content

Thank you for visiting nature.com. You are using a browser version with limited support for CSS. To obtain the best experience, we recommend you use a more up to date browser (or turn off compatibility mode in Internet Explorer). In the meantime, to ensure continued support, we are displaying the site without styles and JavaScript.

  • Letter
  • Published:

L-A virus at 3.4 Å resolution reveals particle architecture and mRNA decapping mechanism

Abstract

The structure of the yeast L-A virus was determined by X-ray crystallography at 3.4 Å resolution. The L-A dsRNA virus is 400 Å in diameter and contains a single protein shell of 60 asymmetric dimers of the coat protein, a feature common among the inner protein shells of dsRNA viruses and probably related to their unique mode of transcription and replication. The two identical subunits in each dimer are in non-equivalent environments and show substantially different conformations in specific surface regions. The L-A virus decaps cellular mRNA to efficiently translate its own uncapped mRNA. Our structure reveals a trench at the active site of the decapping reaction and suggests a role for nearby residues in the reaction.

This is a preview of subscription content, access via your institution

Access options

Buy this article

Prices may be subject to local taxes which are calculated during checkout

Figure 1: Structure of L-A virus particle.
Figure 2
Figure 3: A stereo view ribbon drawing of the side view of molecule A showing the trench accessible from the outside of the L-A particle.
Figure 4: A stereo view close-up of the trench showing residue His 154 and its neighboring residues around the active site.

Similar content being viewed by others

Accession codes

Accessions

Protein Data Bank

References

  1. Wickner, R.B. in Fields Virology 4th edn (eds Knipe, D.M. & Howley, P.M.) 629–658 (Lippincott, Philadelphia; 2001).

    Google Scholar 

  2. Caston, J.R. et al. J. Cell. Biol. 138, 975–985 (1997).

    Article  CAS  Google Scholar 

  3. Ribas, J.C. & Wickner, R.B. J. Biol. Chem. 273, 9306–9311 (1998).

    Article  CAS  Google Scholar 

  4. Fujimura, T., Ribas, J.C., Makhov, A.M. & Wickner, R.B. Nature 359, 746–749 (1992).

    Article  CAS  Google Scholar 

  5. Muhlrad, D., Decker, C.J. & Parker, R. Mol. Cell. Biol. 15, 2145–2156 (1995).

    Article  CAS  Google Scholar 

  6. Blanc, A., Goyer, C. & Sonenberg, N. Mol. Cell. Biol. 12, 3390–3398 (1992).

    Article  CAS  Google Scholar 

  7. Masison, D.C. et al. Mol. Cell. Biol. 15, 2763–2771 (1995).

    Article  CAS  Google Scholar 

  8. Grimes, J.M. et al. Nature 395, 470–478 (1998).

    Article  CAS  Google Scholar 

  9. Reinisch, K.M., Nibert, M.L. & Harrison, S.C. Nature 404, 960–967 (2000).

    Article  CAS  Google Scholar 

  10. Blanc, A., Ribas, J.C., Wickner, R.B. & Sonenberg, N. Mol. Cell. Biol. 14, 2664–2674 (1994).

    Article  CAS  Google Scholar 

  11. Hakansson, K., Doherty, A.J., Shuman, S. & Wigley, D.B. Cell 89, 545–553 (1997).

    Article  CAS  Google Scholar 

  12. Gouet, P. et al. Cell 97, 481–490 (1999).

    Article  CAS  Google Scholar 

  13. Holm, L. & Sander, C. Science 273, 595–603 (1996).

    Article  CAS  Google Scholar 

  14. Koonin, E.V. Semin. Virol. 3, 327–339 (1992).

    CAS  Google Scholar 

  15. Fujimura, T., Esteban, R. & Wickner, R.B. Proc. Natl. Acad. Sci. USA 83, 4433–4437 (1986).

    Article  CAS  Google Scholar 

  16. Uptain, S.M., Kane, C.M. & Chamberlin, M.J. Annu. Rev. Biochem 66, 117–172 (1997).

    Article  CAS  Google Scholar 

  17. Lundquist, R.E., Ehrenfeld, E. & Maizel, J.V. Jr Proc. Natl. Acad. Sci. USA 71, 4773–4477 (1974).

    Article  CAS  Google Scholar 

  18. Zarbl, H. & Millward, S. in The Reoviridae (ed. Joklik, W.K.) 107–196 (Plenum; Dordrecht; 1983).

    Book  Google Scholar 

  19. Naitow, H., Canady, M.A., Lin, T., Wickner, R.B. & Johnson, J.E. J. Struct. Biol. 135, 1–7 (2001).

    Article  CAS  Google Scholar 

  20. Icho, T. & Wickner, R.B. J. Biol. Chem. 264, 6716–6723 (1989).

    CAS  PubMed  Google Scholar 

  21. Diamond, M.E. et al. J. Virol. 63, 3983–3990 (1989).

    CAS  PubMed  PubMed Central  Google Scholar 

  22. Otwinowski, Z. & Minor, W. Methods Enzymol. 277, 505–524 (1997).

    Article  Google Scholar 

  23. Tong, L. & Rossmann, M.G. Methods Enzymol. 276, 594–611 (1997).

    Article  CAS  Google Scholar 

  24. Kleywegt, G.J. & Read, R.J. Structure 5, 1557–1569 (1997).

    Article  CAS  Google Scholar 

  25. Collaborative Computational Project, Number 4 Acta Crystallogr. D 50, 760–763 (1994).

  26. Read, R.J. Acta Crystallogr. A 42, 140–149 (1986).

    Article  Google Scholar 

  27. Jones, T.A., Zou, J.Y., Cowan, S.W. & Kjeldgaard, M. Acta Crystallogr. A 47, 110–119 (1991).

    Article  Google Scholar 

  28. Brünger, A.T. X-PLOR, version 3.1. (Yale University Press, New Haven; 1992).

    Google Scholar 

  29. Laskowski, R.A., MacArthur, M.W., Moss, D.S. & Thornton, J.M. J. Appl. Crystallogr. 26, 283–291 (1993).

    Article  CAS  Google Scholar 

  30. Sayle, R.A. & Milner-White, E.J. Trends Biochem. Sci. 20, 374 (1995).

  31. Kraulis, P.J. J. Appl. Crystallogr. 24, 946–950 (1991).

    Article  Google Scholar 

Download references

Acknowledgements

We thank T. Lin and G. Cingolani for their help in the data collection. Use of the Advanced Photon Source was supported by the U.S. Department of Energy, Basic Energy Sciences, Office of Science. Use of the BioCARS Sector 14 was supported by the National Institutes of Health, National Center for Research Resources. The crystallographic studies were supported by a grant from the National Institutes of Health to J.E.J.

Author information

Authors and Affiliations

Authors

Corresponding author

Correspondence to John E. Johnson.

Ethics declarations

Competing interests

The authors declare no competing financial interests.

Rights and permissions

Reprints and permissions

About this article

Cite this article

Naitow, H., Tang, J., Canady, M. et al. L-A virus at 3.4 Å resolution reveals particle architecture and mRNA decapping mechanism. Nat Struct Mol Biol 9, 725–728 (2002). https://doi.org/10.1038/nsb844

Download citation

  • Received:

  • Accepted:

  • Published:

  • Issue Date:

  • DOI: https://doi.org/10.1038/nsb844

This article is cited by

Search

Quick links

Nature Briefing

Sign up for the Nature Briefing newsletter — what matters in science, free to your inbox daily.

Get the most important science stories of the day, free in your inbox. Sign up for Nature Briefing