ArticlePloS one2013
Crystal structure, SAXS and kinetic mechanism of hyperthermophilic ADP-dependent glucokinase from Thermococcus litoralis reveal a conserved mechanism for catalysis.
Article in PloS one, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.
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13 citing papers in PubMed, 26 citations in OpenAlex.
- Structural Characterization of Glycerol Kinase from the Thermophilic FungusInternational journal of molecular sciences · 2020Article
- Mechanisms of ligand binding.Biophysics reviews · 2020Review
- Crystal Structure ofInternational journal of molecular sciences · 2019Article
- A Phosphofructokinase Homolog from Pyrobaculum calidifontis Displays Kinase Activity towards Pyrimidine Nucleosides and Ribose 1-Phosphate.Journal of bacteriology · 2018Article
- Structural basis for ADP-dependent glucokinase inhibition by 8-bromo-substituted adenosine nucleotide.The Journal of biological chemistry · 2018Article
- Crystal structure of ADP-dependent glucokinase from Methanocaldococcus jannaschii in complex with 5-iodotubercidin reveals phosphoryl transfer mechanism.Protein science : a publication of the Protein Society · 2018Article
- Reconstructed ancestral enzymes reveal that negative selection drove the evolution of substrate specificity in ADP-dependent kinases.The Journal of biological chemistry · 2017Article
- The Structural and Functional Characterization of Mammalian ADP-dependent Glucokinase.The Journal of biological chemistry · 2016Article
- Identifying sequential substrate binding at the single-molecule level by enzyme mechanical stabilization.ACS nano · 2015Article
- Both protein dynamics and ligand concentration can shift the binding mechanism between conformational selection and induced fit.Proceedings of the National Academy of Sciences of the United States of America · 2014Article
- Essential role of conformational selection in ligand binding.Biophysical chemistry · 2014Review
- Conformational selection is a dominant mechanism of ligand binding.Biochemistry · 2013Article
- Structure of an ancestral ADP-dependent kinase with fructose-6P reveals key residues for binding, catalysis, and ligand-induced conformational changes.The Journal of biological chemistryArticle
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6 authors at 2 institutions in 2 countries.
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Abstract
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.
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