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Related Experiment Videos

Fibrinogen substrate recognition by staphylocoagulase.(pro)thrombin complexes.

Peter Panizzi1, Rainer Friedrich, Pablo Fuentes-Prior

  • 1Department of Pathology, Vanderbilt University School of Medicine, Nashville, TN 37232, USA.

The Journal of Biological Chemistry
|October 19, 2005
PubMed
Summary
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Staphylocoagulase (SC) activates prothrombin (ProT) to form a complex that efficiently cleaves fibrinogen (Fbg). This interaction reveals a new binding site, explaining SC

Area of Science:

  • Biochemistry and Molecular Biology
  • Structural Biology
  • Microbiology

Background:

  • Blood coagulation involves thrombin generation and fibrinogen (Fbg) clotting.
  • Staphylocoagulase (SC) from Staphylococcus aureus activates prothrombin (ProT) without proteolysis.
  • Previous structures showed SC binding to prethrombin 2, blocking key sites.

Purpose of the Study:

  • To elucidate the mechanism of fibrinogen binding and cleavage by the SC-prothrombin complex.
  • To characterize the structural basis for high-affinity fibrinogen interaction.
  • To understand the role of this interaction in Staphylococcus aureus endocarditis.

Main Methods:

  • Utilized active site-labeled fluorescent prothrombin analogs.
  • Quantified fibrinogen binding to the SC-(1-325)-ProT complex.

Related Experiment Videos

  • Generated crystal structures of SC-(1-325)-(pre)thrombin complexes and a molecular model of the pentameric complex.

    • Main Results:

    • A novel fibrinogen-binding exosite is expressed on the SC-(1-325)-ProT complex.
    • Formation of a stable pentameric complex ((SC-(1-325).ProT)2.Fbg) with high affinity (Kd = 8-34 nM).
    • Crystal structures revealed dimeric SC-(pre)thrombin complexes with a U-shaped cleft facilitating substrate threading.

    Conclusions:

    • SC-prothrombin complexes bind and cleave fibrinogen with high affinity via a newly identified exosite.
    • A dimeric complex model explains efficient fibrinogen conversion and coagulant properties.
    • This mechanism is crucial for the pathogenesis of Staphylococcus aureus endocarditis.