ArticleJournal of bacteriology2004
Crystal structures of Escherichia coli ATP-dependent glucokinase and its complex with glucose.
Article in Journal of bacteriology, 2004. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 39 papers.
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Who cites it
39 citing papers in PubMed, 92 citations in OpenAlex.
- Glucose repression ofbioRxiv : the preprint server for biology · 2026Article
- Crystal structures of Escherichia coli glucokinase acetylation-mimicking variants and insights into the impact of acetylation.Acta crystallographica. Section F, Structural biology communications · 2026Article
- Characterisation of a cold-adapted, thermostable glucokinase from psychrophilic Pseudoalteromonas sp. AS-131 reveals how the enzyme achieves high thermal stability without loss of cold adaptation.The FEBS journal · 2026Article
- The return of metabolism: biochemistry and physiology of glycolysis.Biological reviews of the Cambridge Philosophical Society · 2026Review
- Mechanistic insights into a cold-adapted glucokinase with high thermal stability were revealed by site-directed spin labeling ESR.Biophysics and physicobiology · 2026Article
- Crystal structures of Escherichia coli glucokinase and insights into phosphate binding.Acta crystallographica. Section F, Structural biology communications · 2025Article
- Engineered3 Biotech · 2024Article
- Neofunctionalization of Glycolytic Enzymes: An Evolutionary Route to Plant Parasitism in the OomyceteMicroorganisms · 2022Article
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- Efficient production of myo-inositol in Escherichia coli through metabolic engineering.Microbial cell factories · 2020Article
- The basis for non-canonical ROK family function in theThe Journal of biological chemistry · 2020Article
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- ATP- and Polyphosphate-Dependent Glucokinases from Aerobic Methanotrophs.Microorganisms · 2019Article
- One pot synthesis of GDP-mannose by a multi-enzyme cascade for enzymatic assembly of lipid-linked oligosaccharides.Biotechnology and bioengineering · 2018Article
- Characterization of the biosynthetic gene cluster (ata) for the A201A aminonucleoside antibiotic from Saccharothrix mutabilis subsp. capreolus.The Journal of antibiotics · 2017Article
- Transcriptomic analysis of a classical model of carbon catabolite regulation in Streptomyces coelicolor.BMC microbiology · 2016Article
- Structure-based approach to the identification of a novel group of selective glucosamine analogue inhibitors of Trypanosoma cruzi glucokinase.Molecular and biochemical parasitology · 2015Article
- Isolation, structural analysis, and expression characteristics of the maize (Zea mays L.) hexokinase gene family.Molecular biology reports · 2014Article
- Carbohydrate metabolism in Archaea: current insights into unusual enzymes and pathways and their regulation.Microbiology and molecular biology reviews : MMBR · 2014Review
- Regulation Systems of Bacteria such as Escherichia coli in Response to Nutrient Limitation and Environmental Stresses.Metabolites · 2013Article
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Authors and funding
6 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Intracellular glucose in Escherichia coli cells imported by phosphoenolpyruvate-dependent phosphotransferase system-independent uptake is phosphorylated by glucokinase by using ATP to yield glucose-6-phosphate. Glucokinases (EC 2.7.1.2) are functionally distinct from hexokinases (EC 2.7.1.1) with respect to their narrow specificity for glucose as a substrate. While structural information is available for ADP-dependent glucokinases from Archaea, no structural information exists for the large sequence family of eubacterial ATP-dependent glucokinases. Here we report the first structure determination of a microbial ATP-dependent glucokinase, that from E. coli O157:H7. The crystal structure of E. coli glucokinase has been determined to a 2.3-A resolution (apo form) and refined to final Rwork/Rfree factors of 0.200/0.271 and to 2.2-A resolution (glucose complex) with final Rwork/Rfree factors of 0.193/0.265. E. coli GlK is a homodimer of 321 amino acid residues. Each monomer folds into two domains, a small alpha/beta domain (residues 2 to 110 and 301 to 321) and a larger alpha+beta domain (residues 111 to 300). The active site is situated in a deep cleft between the two domains. E. coli GlK is structurally similar to Saccharomyces cerevisiae hexokinase and human brain hexokinase I but is distinct from the ADP-dependent GlKs. Bound glucose forms hydrogen bonds with the residues Asn99, Asp100, Glu157, His160, and Glu187, all of which, except His160, are structurally conserved in human hexokinase 1. Glucose binding results in a closure of the small domains, with a maximal Calpha shift of approximately 10 A. A catalytic mechanism is proposed that is consistent with Asp100 functioning as the general base, abstracting a proton from the O6 hydroxyl of glucose, followed by nucleophilic attack at the gamma-phosphoryl group of ATP, yielding glucose-6-phosphate as the product.
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