ArticleThe Journal of biological chemistry2010
Crystal structure of hexokinase KlHxk1 of Kluyveromyces lactis: a molecular basis for understanding the control of yeast hexokinase functions via covalent modification and oligomerization.
Article in The Journal of biological chemistry, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.
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21 citing papers in PubMed, 30 citations in OpenAlex.
- Trehalose-6-phosphate synthase promotes thermotolerance by governing glycolytic flux inbioRxiv : the preprint server for biology · 2026Article
- Exploring the conformational landscape of adenylate kinase and beyond with protein folding models.Scientific reports · 2026Article
- Worth the Weight: Sub-Pocket EXplorer (SubPEx), a Weighted Ensemble Method to Enhance Binding-Pocket Conformational Sampling.Journal of chemical theory and computation · 2023Article
- Structural Analysis ofInternational journal of molecular sciences · 2023Article
- Worth the weight: Sub-Pocket EXplorer (SubPEx), a weighted-ensemble method to enhance binding-pocket conformational sampling.bioRxiv : the preprint server for biology · 2023Article
- Changing course: Glucose starvation drives nuclear accumulation of Hexokinase 2 in S. cerevisiae.PLoS genetics · 2023Article
- Novel mutation in hexokinase 2 confers resistance to 2-deoxyglucose by altering protein dynamics.PLoS computational biology · 2022Article
- Genetic and Physiological Characterization of Fructose-1,6-Bisphosphate Aldolase and Glyceraldehyde-3-Phosphate Dehydrogenase in the Crabtree-Negative YeastInternational journal of molecular sciences · 2022Article
- A 37-amino acid loop in the Yarrowia lipolytica hexokinase impacts its activity and affinity and modulates gene expression.Scientific reports · 2021Article
- Moonlighting Proteins: The Case of the Hexokinases.Frontiers in molecular biosciences · 2021Review
- Article
- Polymerization in the actin ATPase clan regulates hexokinase activity in yeast.Science (New York, N.Y.) · 2020Article
- Crystal Structure ofInternational journal of molecular sciences · 2019Article
- The catalytic inactivation of the N-half of human hexokinase 2 and structural and biochemical characterization of its mitochondrial conformation.Bioscience reports · 2018Article
- Regulatory Function of Hexokinase 2 in Glucose Signaling in Saccharomyces cerevisiae.The Journal of biological chemistry · 2016Article
- Involvement of Arabidopsis Hexokinase1 in Cell Death Mediated by Myo-Inositol Accumulation.The Plant cell · 2015Article
- Protein kinase Ymr291w/Tda1 is essential for glucose signaling in saccharomyces cerevisiae on the level of hexokinase isoenzyme ScHxk2 phosphorylation*.The Journal of biological chemistry · 2015Article
- Proteomic and functional consequences of hexokinase deficiency in glucose-repressible Kluyveromyces lactis.Molecular & cellular proteomics : MCP · 2014Article
- Structural insight into activation mechanism of Toxoplasma gondii nucleoside triphosphate diphosphohydrolases by disulfide reduction.The Journal of biological chemistry · 2012Article
- Molecular mechanism of selective substrate engagement and inhibitor disengagement of cysteine synthase.The Journal of biological chemistryArticle
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Authors and funding
11 authors at 4 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Crystal structures of the unique hexokinase KlHxk1 of the yeast Kluyveromyces lactis were determined using eight independent crystal forms. In five crystal forms, a symmetrical ring-shaped homodimer was observed, corresponding to the physiological dimer existing in solution as shown by small-angle x-ray scattering. The dimer has a head-to-tail arrangement such that the small domain of one subunit interacts with the large domain of the other subunit. Dimer formation requires favorable interactions of the 15 N-terminal amino acids that are part of the large domain with amino acids of the small domain of the opposite subunit, respectively. The head-to-tail arrangement involving both domains of the two KlHxk1 subunits is appropriate to explain the reduced activity of the homodimer as compared with the monomeric enzyme and the influence of substrates and products on dimer formation and dissociation. In particular, the structure of the symmetrical KlHxk1 dimer serves to explain why phosphorylation of conserved residue Ser-15 may cause electrostatic repulsions with nearby negatively charged residues of the adjacent subunit, thereby inducing a dissociation of the homologous dimeric hexokinases KlHxk1 and ScHxk2. Two complex structures of KlHxk1 with bound glucose provide a molecular model of substrate binding to the open conformation and the subsequent classical domain closure motion of yeast hexokinases. The entirety of the novel data extends the current concept of glucose signaling in yeast and complements the induced-fit model by integrating the events of N-terminal phosphorylation and dissociation of homodimeric yeast hexokinases.
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