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Crystal Structure, SAXS and Kinetic Mechanism of Hyperthermophilic ADP-Dependent Glucokinase from Thermococcus litoralis Reveal a Conserved Mechanism for Catalysis

AutorRivas-Pardo, J. A.; Herrera-Morande, A. ; Castro-Fernández, V.; Fernández, Francisco J. ; Vega, María Cristina ; Guixé, V.
Palabras claveBiocatalysis
Crystal structure
Enzyme kinetics
Enzyme structure
Enzymes
Glucose
Protein interactions
Fecha de publicación20-jun-2013
EditorPublic Library of Science
CitaciónPLoS ONE 8(6):e66687
Resumen[EN]ADP-dependent glucokinases represent a unique family of kinases that belong to the ribokinase superfamily, being present mainly in hyperthermophilic archaea. For these enzymes there is no agreement about the magnitude of the structural transitions associated with ligand binding and whether they are meaningful to the function of the enzyme. We used the ADP-dependent glucokinase from Termococcus litoralis as a model to investigate the conformational changes observed in X-ray crystallographic structures upon substrate binding and to compare them with those determined in solution in order to understand their interplay with the glucokinase function. Initial velocity studies indicate that catalysis follows a sequential ordered mechanism that correlates with the structural transitions experienced by the enzyme in solution and in the crystal state. The combined data allowed us to resolve the open-closed conformational transition that accounts for the complete reaction cycle and to identify the corresponding clusters of aminoacids residues responsible for it. These results provide molecular bases for a general mechanism conserved across the ADP-dependent kinase family
Versión del editorhttp://dx.doi.org/10.1371/journal.pone.0066687
URIhttp://hdl.handle.net/10261/95792
DOI10.1371/journal.pone.0066687
ISSN1932-6203
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