Thermodynamic analysis of substrate induced domain closure of 3-phosphoglycerate kinase

Andrea Varga, Judit Szabó, Beáta Flachner, Zoltán Gugolya, Ferenc Vonderviszt, Péter Závodszky, Mária Vas

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10 Citations (Scopus)


The energetic changes accompanying domain closure of 3-phosphoglycerate kinase, a typical hinge-bending enzyme, were assessed. Calorimetric titrations of the enzyme with each substrate, both in the absence and presence of the other one, provide information not only about the energetics of substrate binding, but of the associated conformational changes, including domain closure. Our results suggest that conformational rearrangements in the hinge generated by binding of both substrates provide the main driving force for domain closure overcoming the slightly unfavourable contact interactions between the domains.

Original languageEnglish
Pages (from-to)3660-3664
Number of pages5
JournalFEBS letters
Issue number22
Publication statusPublished - Nov 19 2009



  • Domain closure
  • Energetic parameters
  • Isothermal titration calorimetry
  • Phosphoglycerate kinase
  • Substrate binding

ASJC Scopus subject areas

  • Biophysics
  • Structural Biology
  • Biochemistry
  • Molecular Biology
  • Genetics
  • Cell Biology

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