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A novel solenoid fold in the cell wall anchoring domain of the pneumococcal virulence factor LytA

Nature Structural Biology volume 8, pages 1020–1024 (2001)Cite this article

Abstract

Choline binding proteins are virulence determinants present in several Gram-positive bacteria. Because anchorage of these proteins to the cell wall through their choline binding domain is essential for bacterial virulence, their release from the cell surface is considered a powerful target for a weapon against these pathogens. The first crystal structure of a choline binding domain, from the toxin-releasing enzyme pneumococcal major autolysin (LytA), reveals a novel solenoid fold consisting exclusively of β-hairpins that stack to form a left-handed superhelix. This unique structure is maintained by choline molecules at the hydrophobic interface of consecutive hairpins and may be present in other choline binding proteins that share high homology to the repeated motif of the domain.

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Figure 1: The crystal structure of LytA ChBD.
Figure 2: Sequence and structural similarities among repeats.
Figure 3: Choline binding sites.
Figure 4: A potential binding surface and the relevance to other ChBPs.

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References

  1. Tettelin, H. et al. Science 293, 498–506 (2001).

    Article  CAS  Google Scholar 

  2. Campbell G.D. Jr., & Silberman, R. Clin. Infect. Dis. 26, 1188–1195 (1998).

    Article  Google Scholar 

  3. Lipsitch, M. Emerg. Infect. Dis. 5, 336–345 (1999).

    Article  CAS  Google Scholar 

  4. Hollingshead, S.K. & Briles, D.E. Curr. Opin. Microbiol. 4, 71–77 (2001).

    Article  CAS  Google Scholar 

  5. Fischer, W. In Streptococcus pneumoniae (ed. Tomasz, A.) 155–177 (Mary Ann Liebert, Inc., Larchmont; 2000).

    Google Scholar 

  6. Wren, B.W. Mol. Microbiol. 5, 797–803 (1991).

    Article  CAS  Google Scholar 

  7. Tu, A.T., Fulgham, R.L., McCrory, M.A., Briles, D.E. & Szalai, A.J. Infect. Immun. 67, 4720–4724 (1999).

    CAS  PubMed  PubMed Central  Google Scholar 

  8. Gosink, K.K., Mann, E.R., Guglielmo, C., Tuomanen, E.I. & Masure, H.R. Infect. Immun. 68, 5690–5695 (2000).

    Article  CAS  Google Scholar 

  9. Mosser, J.L. & Tomasz, A. J. Biol. Chem. 245, 287–298 (1970).

    CAS  PubMed  Google Scholar 

  10. Berry, A.M. & Paton, J.C. Infect. Immun. 68, 133–140 (2000).

    Article  CAS  Google Scholar 

  11. Sánchez-Puelles, J.M., Sanz, J.M., García, J.L. & García, E. Gene 89, 69–75 (1990).

    Article  Google Scholar 

  12. García, E., García, J.L., Ronda, C., García, P. & López, R. Mol. Gen. Genet. 201, 225–230 (1985).

    Article  Google Scholar 

  13. García, E. et al. Proc. Natl. Acad. Sci. USA 85, 914–918 (1988).

    Article  Google Scholar 

  14. Pfam Web Page http://www.Sanger.ac.uk/Software/Pfam/ (2001).

  15. Kobe, B. & Kajava, A.V. TIBS 25, 509–515 (2000).

    CAS  PubMed  Google Scholar 

  16. Holm, L. & Sander, C. J. Mol. Biol. 233, 123 (1993).

  17. von Eichel-Streiber, C., Sauerborn, M. & Kuramitsu, H.K. J. Bacteriol. 174, 6707–6710 (1992).

    Article  CAS  Google Scholar 

  18. Varea, J. et al. J. Biol. Chem. 275, 26842–26855 (2000).

    CAS  PubMed  Google Scholar 

  19. Dougherty, D.A. & Stauffer, D.A. Science 250, 1558–1560 (1990).

    Article  CAS  Google Scholar 

  20. Brown, M., Schumacher, M.A., Wiens, G.D., Brennan, R.G. & Rittenberg, M.B. J. Exp. Med. 191, 2101–2111 (2000).

    Article  CAS  Google Scholar 

  21. Sussman, J.L. et al. Science 253, 872–979 (1991).

    Article  CAS  Google Scholar 

  22. Hajduk, P.J., Meadows, R.P. & Fesik, S.W. Science 278, 497–499 (1997).

    Article  CAS  Google Scholar 

  23. López, R., García, E., García, P. & García, J.L. Microb. Drug Res. 3, 199–211 (1997).

    Article  Google Scholar 

  24. Leslie, A.G.W. In Crystallographic computing V (eds. Moras, D., Podjarny, A.D. & Thierry, J.C.) 27–38 (Oxford University Press, Oxford; 1991).

    Google Scholar 

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

  26. Brünger, A.T. et al. Acta Crystallogr. D 54, 905–921 (1998).

    Article  Google Scholar 

  27. de La Fortelle, E. & Bricogne, G. Methods Enzymol. 276, 472–494 (1997).

    Article  CAS  Google Scholar 

  28. Kraulis, P. J. Appl. Crystallogr. 24, 946–950 (1996).

    Article  Google Scholar 

  29. Barton, G.J. Protein Eng. 6, 37–40 (1993).

    Article  CAS  Google Scholar 

  30. Nicholls, A., Sharp, K.A. & Honig, B. Proteins 11, 281–296 (1991).

    Article  CAS  Google Scholar 

Download references

Acknowledgements

We thank the staff of beamlines X11, X31 and BW7A, at EMBL-DESY (Hamburg) for support. We are grateful to C. Fernández-Cabrera for excellent technical assistance, P. García and E. Pineda-Molina for helpful discussion, and J.L. García and D. Laurents for critical reading of the manuscript. The first author was supported by a predoctoral fellowship from Ministerio de Educación y Ciencia and by a grant in the Residencia de Estudiantes. This work was partially supported by grants from the Ministerio de Educación y Ciencia of Spain.

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Authors and Affiliations

  1. Departamento de Estructura y Función de Proteínas, Centro de Investigaciones Biológicas – CSIC, C/ Velázquez 144, Madrid, 28006, Spain

    Carlos Fernández-Tornero, Guillermo Giménez-Gallego & Antonio Romero

  2. Departamento de Microbiología Molecular, Centro de Investigaciones Biológicas – CSIC, C/ Velázquez 144, Madrid, 28006, Spain

    Rubens López & Ernesto García

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  1. Carlos Fernández-Tornero
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Correspondence to Antonio Romero.

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Fernández-Tornero, C., López, R., García, E. et al. A novel solenoid fold in the cell wall anchoring domain of the pneumococcal virulence factor LytA. Nat Struct Mol Biol 8, 1020–1024 (2001). https://doi.org/10.1038/nsb724

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