Thermodynamic analysis of substrate induced domain closure of 3-phosphoglycerate kinase |
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| Authors: | Andrea Varga Judit Szabó Beáta Flachner Ferenc Vonderviszt Péter Závodszky |
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| Institution: | a Institute of Enzymology, Biological Research Center, Hungarian Academy of Sciences, P.O. Box 7, H-1518 Budapest, Hungary
b University of Pannonia, Faculty of Information Technology, Department of Nanotechnology, P.O. Box 158, H-8201 Veszprém, Hungary |
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| Abstract: | 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. |
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| Keywords: | Domain closure Phosphoglycerate kinase Isothermal titration calorimetry Substrate binding Energetic parameters |
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