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Related Experiment Videos

Structural changes of creatine kinase upon substrate binding

M Forstner1, M Kriechbaum, P Laggner

  • 1Institute of Cell Biology, Swiss Federal Institute of Technology Zürich, CH-8093 Zürich, Switzerland. forstner1@llnl.gov

Biophysical Journal
|July 24, 1998
PubMed
Summary
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Structural changes in creatine kinase (CK) and arginine kinase (AK) were observed upon substrate binding. Mg-nucleotide binding induced significant conformational changes in both enzymes, affecting their size and shape.

Area of Science:

  • Biochemistry
  • Structural Biology
  • Enzymology

Background:

  • Creatine kinase (CK) and arginine kinase (AK) are enzymes crucial for energy metabolism.
  • Understanding enzyme structural dynamics upon substrate binding is key to elucidating their catalytic mechanisms.

Purpose of the Study:

  • To investigate the structural alterations in CK isoenzymes and AK upon binding of substrates or a transition state analog complex (TSAC).
  • To compare the structural responses of dimeric M-CK, octameric Mi-CK, and monomeric AK to ligand binding.

Main Methods:

  • Small-angle X-ray scattering (SAXS) was employed to measure changes in the radius of gyration.
  • Enzymes studied included muscle-type CK (M-CK), mitochondrial CK (Mi-CK), and arginine kinase (AK).
  • Ligands included individual substrates, Mg-nucleotides (Mg-ATP, Mg-ADP), and a transition state analog complex (TSAC).

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Main Results:

  • Mg-nucleotide or TSAC binding caused considerable changes in the size and shape of both CK and AK.
  • Mi-CK's radius of gyration decreased from 55.6 Å (free) to 48.9 Å (Mg-ATP) and 48.2 Å (TSAC).
  • M-CK showed similar reductions from 28.0 Å (free) to 25.6 Å (Mg-ATP) and 25.5 Å (TSAC).
  • AK's radius of gyration decreased from 21.5 Å (free) to 19.7 Å (Mg-ATP).
  • Individual substrates (creatine, arginine) induced only minor structural changes.

Conclusions:

  • Mg-nucleotide binding induces significant conformational changes, primarily domain movements, in monomeric AK.
  • CK enzymes exhibit more complex structural rearrangements beyond simple domain movements upon ligand binding.
  • These findings provide insights into the allosteric regulation and catalytic mechanisms of these kinases.