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Related Experiment Videos

Induced fit in arginine kinase.

G Zhou1, W R Ellington, M S Chapman

  • 1Institute of Molecular Biophysics, Florida State University, Tallahassee, Florida 32306-4380, USA.

Biophysical Journal
|February 29, 2000
PubMed
Summary

Creatine kinase (CK) and arginine kinase (AK) enzymes undergo significant structural changes upon substrate binding. These conformational shifts are crucial for efficient energy metabolism and catalysis by aligning substrates and preventing wasteful reactions.

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Area of Science:

  • Biochemistry
  • Structural Biology
  • Enzymology

Background:

  • Creatine kinase (CK) and arginine kinase (AK) are key enzymes in cellular energy buffering.
  • They play a central role in energy metabolism by managing ATP levels.
  • These enzymes are considered paradigms in classical enzymology.

Purpose of the Study:

  • To compare the structural differences between substrate-free and substrate-bound states of CK and AK.
  • To investigate substrate-induced conformational changes in these enzymes.
  • To understand the functional implications of these structural alterations in catalysis.

Main Methods:

  • Comparative structural analysis of creatine kinase (CK) and arginine kinase (AK).
  • Examination of open (substrate-free) and closed (substrate-bound) enzyme structures.
  • Analysis of domain rotation and loop ordering in response to substrate binding.

Main Results:

  • Significant conformational changes observed upon substrate binding, consistent with biophysical evidence.
  • A hinged rotation of 13 degrees between large and small domains was identified.
  • Specific loops, including residues 309-319, reposition to cover substrates, moving up to 15 Å.
  • Active site configuration and water exclusion are regulated by these conformational changes.

Conclusions:

  • Substrate-induced conformational changes in CK and AK are essential for efficient catalysis.
  • These dynamic structural alterations facilitate substrate alignment and active site formation.
  • The conformational changes prevent wasteful ATP hydrolysis by excluding water from the active site.

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