Skip to main content
SpringerLink
Log in

Structural basis for dimerization of the Dictyostelium gelation factor (ABP120) rod

  • Letter
  • Published:

From Nature Structural Biology

View current issue Submit your manuscript

Abstract

Gelation factor (ABP120) is one of the principal actin-cross-linking proteins of Dictyostelium discoideum. The extended molecule has an N-terminal 250-residue actin-binding domain and a rod constructed from six 100-residue repeats that have an Ig fold. The ability to dimerize is crucial to the actin cross-linking function of gelation factor and is mediated by the rod in which the two chains are arranged in an antiparallel fashion. We report the 2.2 Å resolution crystal structure of rod domains 5 and 6, which shows that dimerization is mediated primarily by rod domain 6 and is the result of a double edge-to-edge extension of β-sheets. Thus, contrary to earlier proposals, the chains of the dimeric gelation factor molecule overlap only within domain 6, and domains 1–5 do not pair with domains from the other chain. This information allows construction of a model of the gelation factor molecule and suggests how the chains in the related molecule filamin (ABP280) may interact.

This is a preview of subscription content, log in via an institution to check access.

Access this article

Log in via an institution

Price excludes VAT (USA)
Tax calculation will be finalised during checkout.

Instant access to the full article PDF.

Institutional subscriptions

Figure 1: Structure of gelation factor.
Figure 2: Topology of gelation factor.
Figure 3: Sigma-A weighted 2Fo - Fc electron density maps.
Figure 4: Sequence alignments of gelation factor and ABP280.
Figure 5: Model of gelation factor.

Similar content being viewed by others

References

  1. Carlier, M.-F. & Pantaloni, D. J. Mol. Biol. 269, 459–467 (1997).

    Article  CAS  PubMed  Google Scholar 

  2. Steinmetz, M.O., Stoffer, D., Hoenger, A., Bremer, A. & Aebi, U. J. Struct. Biol. 119, 295– 320 (1997).

    Article  CAS  PubMed  Google Scholar 

  3. Puius, Y.A., Mahoney, N.M. & Almo, S.C. Curr. Opin. Cell Biol. 10, 23–34 (1998).

    Article  CAS  PubMed  Google Scholar 

  4. Fucini, P., Renner, C., Herberhold, C., Noegel, A.A. & Holak, T.A. Nature Struct. Biol. 4, 223–230 (1997).

    Article  CAS  PubMed  Google Scholar 

  5. McGough, A. Curr. Opin. Struct. Biol. 8, 166–176 (1998).

    Article  CAS  PubMed  Google Scholar 

  6. Rivero, F. et al. J. Cell Sci. 109, 2679– 2691 (1996).

    CAS  PubMed  Google Scholar 

  7. Wachsstock, D.H., Schwarz, W.H. & Pollard, T.P. Biophys. J. 66, 801– 809 (1994).

    Article  CAS  PubMed Central  PubMed  Google Scholar 

  8. Goldsmith, S.C. et al. Nature Struct. Biol. 4, 708– 712 (1997).

    Article  CAS  PubMed  Google Scholar 

  9. Brink, M. et al. J. Cell. Biol. 111, 1477– 1489 (1990).

    Article  CAS  PubMed  Google Scholar 

  10. Cox, D. et al. J. Cell Biol. 116, 943–955 (1992).

    Article  CAS  PubMed  Google Scholar 

  11. Cox, D., Risdale, J.A., Condeelis, J. & Hartwig, J. J. Cell Biol. 128, 819–835 (1995).

    Article  CAS  PubMed  Google Scholar 

  12. Witke, W., Schleicher, M. & Noegel, A.A. Cell, 68, 53– 62 (1992).

    Article  CAS  Google Scholar 

  13. Gorlin, J.B. et al. J. Cell Biol. 111, 1089– 1105 (1990).

    Article  CAS  PubMed  Google Scholar 

  14. Cunningham, C.C. et al. Science 255, 325– 327 (1992).

    Article  CAS  PubMed  Google Scholar 

  15. Zhang, W., Han, S.W., McKeel, D.W., Goate, A. & Wu, J.Y. J. Neurosci. 18, 914–922 (1998).

    Article  CAS  PubMed Central  PubMed  Google Scholar 

  16. Condeelis, J., Vahey, M., Carboni, J.M., DeMey, J. & Ogihara, S. J. Cell Biol. 99, 119s– 126s (1984).

    Article  CAS  PubMed Central  PubMed  Google Scholar 

  17. Noegel, A.A., Rapp, S., Lottspeich, F., Schleicher, M., & Stewart, M. J. Cell. Biol. 109, 607– 618 (1989).

    Article  CAS  PubMed  Google Scholar 

  18. Bresnick, A.R., Warren, V. & Condeelis, J. J. Biol. Chem. 265, 9236– 9240 (1990).

    CAS  PubMed  Google Scholar 

  19. Hartwig, J.H. In Protein profile: spectrin superfamily, Vol. 1 (ed. Hartwig, J.H.) 739–746 (Academic Press, New York; 1995).

    Google Scholar 

  20. Fucini, P., McCoy, A.J., Gomez-Ortiz, M., Schleicher, M., & Noegel, A.A. J. Struct. Biol. 120 , 192–195 (1997).

    Article  CAS  PubMed  Google Scholar 

  21. Jones, S. & Thornton, J.M. Proteins 21, 30–39 (1995).

    Article  CAS  Google Scholar 

  22. Williams, A.F. & Barclay, A.N. Annu. Rev. Immunol. 6, 381–405 ( 1988).

    Article  CAS  PubMed  Google Scholar 

  23. Harpaz, Y. & Chothia, C. J. Mol. Biol. 238, 528–539 (1994).

    Article  CAS  PubMed  Google Scholar 

  24. Hamilton, J.A. et al. J. Biol. Chem. 268, 2416– 2424 (1993).

    CAS  PubMed  Google Scholar 

  25. Colman, P.M. Adv. Immunol. 43, 99–132 (1988).

    Article  CAS  PubMed  Google Scholar 

  26. Improta, S. et al. J. Mol. Biol. 284, 761– 777 (1998).

    Article  CAS  PubMed  Google Scholar 

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

  28. de La Fortelle, E. & Bricogne, G. Methods Enzymol. 276, 472–493 ( 1997).

    Article  CAS  PubMed  Google Scholar 

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

    Article  PubMed  Google Scholar 

  30. Esnouf, R.M. J. Mol. Graphics 15, 132–136 (1997).

    Article  CAS  Google Scholar 

  31. Richardson, J.S. Adv. Protein Chem. 34, 167–339 (1981).

    Article  CAS  PubMed  Google Scholar 

Download references

Acknowledgements

We thank A.Thompson, G. Leonard and A. Baker for assistance in collecting MAD data at BL14 at ESRF, Grenoble; R. Muller and H. Kent for assistance with protein preparation and light scattering; A. Murzin, E. de la Fortelle and J. Irwin for advice; and our colleagues in Martinsried and Cambridge, especially M. Schleicher, for their assistance. A.J.M. is a Howard Florey Fellow of the Royal Society of London. P.F. held a short-term EMBO Fellowship, and this work was supported in part by EC CHRX-CT93-0250 and a grant to A.N. from the Centre for Molecular Medicine, Cologne.

Author information

Author notes

  1. Paola Fucini

    Present address: New Chemistry Laboratories, South Parks Rd, Oxford, OX1 3QT, UK

Authors and Affiliations

  1. MRC Laboratory of Molecular Biology, Hills Rd., Cambridge, CB2 2QH, UK

    Airlie J. McCoy & Murray Stewart

  2. Abteilung Zellbiologie, Max-Planck-Institut für Biochemie, Martinsried bei München, D-82152, Germany

    Paola Fucini & Angelika A. Noegel

  3. Institut für Biochemie I, Medizinische Einrichtungen der Universität zu Köln, Joseph-Stelzmann-Strabe 52 , Köln, D-50931, Germany

    Angelika A. Noegel

Authors
  1. Airlie J. McCoy
    View author publications

    You can also search for this author in PubMed Google Scholar

  2. Paola Fucini
    View author publications

    You can also search for this author in PubMed Google Scholar

  3. Angelika A. Noegel
    View author publications

    You can also search for this author in PubMed Google Scholar

  4. Murray Stewart
    View author publications

    You can also search for this author in PubMed Google Scholar

Corresponding author

Correspondence to Murray Stewart.

Rights and permissions

Reprints and permissions

About this article

Cite this article

McCoy, A., Fucini, P., Noegel, A. et al. Structural basis for dimerization of the Dictyostelium gelation factor (ABP120) rod. Nat Struct Mol Biol 6, 836–841 (1999). https://doi.org/10.1038/12296

Download citation

  • Received:

  • Accepted:

  • Issue Date:

  • DOI: https://doi.org/10.1038/12296

  • Springer Nature America, Inc.

This article is cited by

Search

Navigation