Thermodynamic analysis of substrate induced domain closure of 3-phosphoglycerate kinase.
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.
Institute of Enzymology, Biological Research Center, Hungarian Academy of Sciences, PO Box 7, H-1518 Budapest, Hungary.
Andrea
A
Varga
Judit
J
Szabó
Beáta
B
Flachner
Zoltán
Z
Gugolya
Ferenc
F
Vonderviszt
Péter
P
Závodszky
Mária
M
Vas
D000244:Adenosine Diphosphate / Q000737:chemistry / Q000378:metabolism; D000266:Adenylyl Imidodiphosphate / Q000737:chemistry / Q000378:metabolism; D001665:Binding Sites; D005988:Glyceric Acids / Q000737:chemistry / Q000378:metabolism; D006801:Humans; D007700:Kinetics; D016297:Mutagenesis, Site-Directed; D009154:Mutation; D010735:Phosphoglycerate Kinase / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism*; D011485:Protein Binding; D011487:Protein Conformation; D017434:Protein Structure, Tertiary; D013379:Substrate Specificity; D013816:Thermodynamics
D005988:Glyceric Acids; D000266:Adenylyl Imidodiphosphate; D000244:Adenosine Diphosphate; C005156:3-phosphoglycerate; D010735:Phosphoglycerate Kinase