Crystal structure, SAXS and kinetic mechanism of hyperthermophilic ADP-dependent glucokinase from Thermococcus litoralis reveal a conserved mechanism for catalysis.

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...

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Autores principales:	Jaime Andrés Rivas-Pardo, Alejandra Herrera-Morande, Victor Castro-Fernandez, Francisco J Fernandez, M Cristina Vega, Victoria Guixé
Formato:	article
Lenguaje:	EN
Publicado:	Public Library of Science (PLoS) 2013
Materias:	Medicine R Science Q
Acceso en línea:	https://doaj.org/article/b2d8ce230eeb49d3a1e21fe3d7bff364
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spelling	oai:doaj.org-article:b2d8ce230eeb49d3a1e21fe3d7bff3642021-11-18T07:40:57ZCrystal structure, SAXS and kinetic mechanism of hyperthermophilic ADP-dependent glucokinase from Thermococcus litoralis reveal a conserved mechanism for catalysis.1932-620310.1371/journal.pone.0066687https://doaj.org/article/b2d8ce230eeb49d3a1e21fe3d7bff3642013-01-01T00:00:00Zhttps://www.ncbi.nlm.nih.gov/pmc/articles/pmid/23818958/?tool=EBIhttps://doaj.org/toc/1932-6203ADP-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 Thermococcus 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.Jaime Andrés Rivas-PardoAlejandra Herrera-MorandeVictor Castro-FernandezFrancisco J FernandezM Cristina VegaVictoria GuixéPublic Library of Science (PLoS)articleMedicineRScienceQENPLoS ONE, Vol 8, Iss 6, p e66687 (2013)
institution	DOAJ
collection	DOAJ
language	EN
topic	Medicine R Science Q
spellingShingle	Medicine R Science Q Jaime Andrés Rivas-Pardo Alejandra Herrera-Morande Victor Castro-Fernandez Francisco J Fernandez M Cristina Vega Victoria Guixé Crystal structure, SAXS and kinetic mechanism of hyperthermophilic ADP-dependent glucokinase from Thermococcus litoralis reveal a conserved mechanism for catalysis.
description	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 Thermococcus 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.
format	article
author	Jaime Andrés Rivas-Pardo Alejandra Herrera-Morande Victor Castro-Fernandez Francisco J Fernandez M Cristina Vega Victoria Guixé
author_facet	Jaime Andrés Rivas-Pardo Alejandra Herrera-Morande Victor Castro-Fernandez Francisco J Fernandez M Cristina Vega Victoria Guixé
author_sort	Jaime Andrés Rivas-Pardo
title	Crystal structure, SAXS and kinetic mechanism of hyperthermophilic ADP-dependent glucokinase from Thermococcus litoralis reveal a conserved mechanism for catalysis.
title_short	Crystal structure, SAXS and kinetic mechanism of hyperthermophilic ADP-dependent glucokinase from Thermococcus litoralis reveal a conserved mechanism for catalysis.
title_full	Crystal structure, SAXS and kinetic mechanism of hyperthermophilic ADP-dependent glucokinase from Thermococcus litoralis reveal a conserved mechanism for catalysis.
title_fullStr	Crystal structure, SAXS and kinetic mechanism of hyperthermophilic ADP-dependent glucokinase from Thermococcus litoralis reveal a conserved mechanism for catalysis.
title_full_unstemmed	Crystal structure, SAXS and kinetic mechanism of hyperthermophilic ADP-dependent glucokinase from Thermococcus litoralis reveal a conserved mechanism for catalysis.
title_sort	crystal structure, saxs and kinetic mechanism of hyperthermophilic adp-dependent glucokinase from thermococcus litoralis reveal a conserved mechanism for catalysis.
publisher	Public Library of Science (PLoS)
publishDate	2013
url	https://doaj.org/article/b2d8ce230eeb49d3a1e21fe3d7bff364
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Crystal structure, SAXS and kinetic mechanism of hyperthermophilic ADP-dependent glucokinase from Thermococcus litoralis reveal a conserved mechanism for catalysis.

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