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Cooperative allosteric transitions can occur in multimeric proteins, where each subunit of the protein has its own ligand-binding site. When a ligand binds to any of these subunits, it triggers a conformational change that affects the binding sites in the other subunits; this can change the affinity of the other sites for their respective ligands. The ability of the protein to change the shape of its binding site is attributed to the presence of a mix of flexible and stable segments in the...
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Prothrombinase processivity is conferred by substrate allostery.

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The prothrombinase complex uses a novel

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Area of Science:

  • Biochemistry
  • Structural Biology
  • Enzymology

Background:

  • The prothrombinase complex (factor Xa and factor Va) is crucial for blood coagulation.
  • Understanding its mechanism of prothrombin conversion to thrombin is vital.
  • Structural insights into substrate binding are lacking.

Purpose of the Study:

  • To elucidate the molecular basis of prothrombin processing by the prothrombinase complex.
  • To provide structural insights into substrate and intermediate binding.
  • To reveal the enzymatic mechanism of thrombin generation.

Main Methods:

  • Cryo-electron microscopy (cryo-EM) was used to determine structures.
  • Structures of prothrombinase bound to prothrombin and meizothrombin were solved at 3.1 Å resolution.

Main Results:

  • A surprising interaction was found between factor Va heavy chain and prothrombin exosite I.
  • Cleavage at Arg320 induces significant conformational changes in meizothrombin.
  • These changes rearrange the substrate to expose the second cleavage site.

Conclusions:

  • The prothrombinase complex employs a unique mechanism involving substrate participation.
  • A new paradigm of 'substrate allostery' is introduced.
  • This mechanism explains the rapid and processive conversion of prothrombin to thrombin.