Skip to main content
SpringerLink
Log in

NMR secondary structure of the plasminogen activator protein staphylokinase

  • Published:
Journal of Biomolecular NMR Aims and scope Submit manuscript

Abstract

Staphylokinase (Sak) is a 15.5 kDa protein secreted by several strains of Staphylococcusaureus. Due to its ability to convert plasminogen, the inactive proenzyme of the fibrinolyticsystem, into plasmin, Sak is presently undergoing clinical trials for blood clot lysis in thetreatment of thrombovascular disorders. With a view to developing a better understanding ofthe mode of action of Sak, we have initiated a structural investigation of Sak viamultidimensional heteronuclear NMR spectroscopy employing uniformly 15N- and 15N,13C-labelled Sak. Sequence-specific resonance assignments have been made employing 15N-editedTOCSY and NOE experiments and from HNCACB, CBCA(CO)NH, HBHA(CBCACO)NHand CC(CO)NH sets of experiments. From an analysis of the chemical shifts,3JHNHα scalar coupling constants, NOEs and HN exchange data, the secondary structural elements of Sakhave been characterized.

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

Similar content being viewed by others

References

  • Bartels, C., Xia, T., Billeter, M., Güntert, P. and Wüthrich, K. (1995) J. Biomol. NMR, 6, 1–10.

    Google Scholar 

  • Behnke, D. and Gerlach, D. (1987) Mol. Gen. Genet., 210, 528–534.

    Google Scholar 

  • Bodenhausen, G. and Ruben, D.J. (1980) Chem. Phys. Lett., 69, 185–188.

    Google Scholar 

  • Collen, D., Silence, K., Demarsin, E., De Mol, M. and Lijnen, H.R. (1992) Fibrinolysis, 6, 203–213.

    Google Scholar 

  • Collen, D., Schlott, B., Engelbourghs, Y., Van Hoef, B., Hartmann, M., Lijnen, H.R. and Behnke, D. (1993) J. Biol. Chem., 268, 8284–8289.

    Google Scholar 

  • Collen, D. and Van de Werf, F. (1993) Circulation, 87, 1850–1853.

    Google Scholar 

  • Damaschun, G., Damaschun, H., Gast, K., Misselwitz, R., Zirwer, D., Gührs, K.-H., Hartmann, M., Schlott, B., Triebel, H. and Behnke, D. (1993) Biochim. Biophys. Acta, 1161, 244–248.

    Google Scholar 

  • Dornberger, U., Fandrei, D., Backmann, J., Hübner, W., Rahmelow, K., Gührs, K.-H., Hartmann, M., Schlott, B. and Fritzsche, H. (1996) Biochim. Biophys. Acta, 1294, 168–176.

    Google Scholar 

  • Fesik, S.W. and Zuiderweg, E.R.P. (1988) J. Magn. Reson., 78, 588–593.

    Google Scholar 

  • Fujiwara, T., Anai, T., Kurihara, N. and Nagayama, K. (1993) J. Magn. Reson., A104, 103–105.

    Google Scholar 

  • Gase, A., Birch-Hirschfeld, E., Gührs, K.-H., Hartmann, M., Vettermann, S., Damaschun, G., Damaschun, H., Gast, K., Misselwitz, R., Zirwer, D., Collen, D. and Schlott, B. (1994) Eur. J. Biochem., 223, 303–308.

    Google Scholar 

  • Gase, A., Hartmann, M., Gührs, K.-H., Röcker, A., Collen, D., Behnke, D. and Schlott, B. (1996) Thromb. Haemostasis, 76, 755–760.

    Google Scholar 

  • Grzesiek, S. and Bax, A. (1992) J. Am. Chem. Soc., 114, 6291–6293.

    Google Scholar 

  • Grzesiek, S., Anglister, J. and Bax, A. (1993) J. Magn. Reson., B101, 114–119.

    Google Scholar 

  • Grzesiek, S. and Bax, A. (1993) J. Biomol. NMR, 3, 185–204.

    Google Scholar 

  • Kay, L.E., Ikura, M., Tschudin, R. and Bax, A. (1990) J. Magn. Reson., 89, 496–514.

    Google Scholar 

  • Kay, L.E., Xu, G.Y., Singer, A.V., Muhandiram, D.R. and Kay, J. D.F. (1993) J. Magn. Reson., B101, 333–337.

    Google Scholar 

  • Lijnen, H.R., Van Hoef, B., De Cock, F., Okada, K., Ueshima, S., Matsuo, O. and Collen, D. (1991) J. Biol. Chem., 266, 11826–11832.

    Google Scholar 

  • Lijnen, H.R., Van Hoef, B., Vandenbossche, L. and Collen, D. (1992) Fibrinolysis, 6, 214–225.

    Google Scholar 

  • Marion, D., Driscoll, P., Kay, L.E., Wingfield, P., Bax, A., Gronenborn, A. M. and Clore, G.M. (1989) Biochemistry, 28, 6150–6156.

    Google Scholar 

  • McCoy, M.A. and Müller, L. (1993) J. Magn. Reson., A101, 122–130.

    Google Scholar 

  • Pardi, A., Billeter, M. and Wüthrich, K. (1984) J. Mol. Biol., 180, 741–751.

    Google Scholar 

  • Piotto, M., Saudek, V. and Sklenář, V. (1992) J. Biomol. NMR, 2, 661–665.

    Google Scholar 

  • Sako, T., Sawaki, S., Sakurai, T., Ito, S., Yosizawa, Y. and Kondo, I. (1983) Mol. Gen. Genet., 190, 271–277.

    Google Scholar 

  • Schlott, B., Hartmann, M., Gührs, K.-H., Birch-Hirschfeld, E., Gase, A., Vettermann, S., Collen, D. and Lijnen, H.R. (1994a) Biochim. Biophys. Acta, 1204, 235–242.

    Google Scholar 

  • Schlott, B., Hartmann, M., Gührs, K.-H., Birch-Hirschfeld, E., Pohl, H.-D., Vanderschueren, S., Van de Werf, F., Michoel, A., Collen, D. and Behnke, D. (1994b) Biotechnology, 12, 185–189.

    Google Scholar 

  • Shaka, A.J., Barker, P.B. and Freeman, R. (1985) J. Magn. Reson., 64, 547–552.

    Google Scholar 

  • Shaka, A.J., Lee, C.J. and Pines, A. (1988) J. Magn. Reson., 77, 274–293.

    Google Scholar 

  • Silence, K., Collen, D. and Lijnen, H.R. (1993) J. Biol. Chem., 268, 9811–9816.

    Google Scholar 

  • Silence, K., Hartmann, M., Gührs, K.-H., Gase, A., Schlott, B., Collen, D. and Lijnen, H.R. (1995) J. Biol. Chem., 270, 27192–27198.

    Google Scholar 

  • States, D.J., Haberkorn, R.A. and Ruben, D.J. (1982) J. Magn. Reson., 48, 286–292.

    Google Scholar 

  • Vanderschueren, S., Stockx, L., Wilms, G., Lacroix, H., Verhaeghe, R., Vermylen, J. and Collen, D. (1995) Circulation, 92, 2050–2056.

    Google Scholar 

  • Vuister, G.W. and Bax, A. (1993) J. Am. Chem. Soc., 115, 7772–7777.

    Google Scholar 

  • Wishart, D.S., Sykes, B.D. and Richards, F.M. (1992) Biochemistry, 31, 1647–1651.

    Google Scholar 

  • Wishart, D.S. and Sykes, B.D. (1994) J. Biomol. NMR, 4, 171–180.

    Google Scholar 

  • Wittekind, M. and Müller, L. (1993) J. Magn. Reson., B101, 201–205.

    Google Scholar 

  • Zuiderweg, E.R.P. and Fesik, S.W. (1989) Biochemistry, 28, 2387–2391.

    Google Scholar 

Download references

Author information

Authors and Affiliations

  1. Department of Molecular Biophysics/NMR Spectroscopy, Institute of Molecular Biotechnology, P.O. Box 100813, D-07708, Jena, Germany

    O. Ohlenschläger, R. Ramachandran, J. Flemming, K.-H. Gührs, B. Schlott & L.R. Brown

Authors
  1. O. Ohlenschläger
    View author publications

    You can also search for this author in PubMed Google Scholar

  2. R. Ramachandran
    View author publications

    You can also search for this author in PubMed Google Scholar

  3. J. Flemming
    View author publications

    You can also search for this author in PubMed Google Scholar

  4. K.-H. Gührs
    View author publications

    You can also search for this author in PubMed Google Scholar

  5. B. Schlott
    View author publications

    You can also search for this author in PubMed Google Scholar

  6. L.R. Brown
    View author publications

    You can also search for this author in PubMed Google Scholar

Rights and permissions

Reprints and permissions

About this article

Cite this article

Ohlenschläger, O., Ramachandran, R., Flemming, J. et al. NMR secondary structure of the plasminogen activator protein staphylokinase. J Biomol NMR 9, 273–286 (1997). https://doi.org/10.1023/A:1018678925512

Download citation

  • Issue Date:

  • DOI: https://doi.org/10.1023/A:1018678925512

Search

Navigation