ArticleThe Journal of biological chemistry2011
Structure of Streptomyces maltosyltransferase GlgE, a homologue of a genetically validated anti-tuberculosis target.
Article in The Journal of biological chemistry, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 31 papers.
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Who cites it
31 citing papers in PubMed, 61 citations in OpenAlex.
- Genomic insights into biosynthesis and adaptation in the bioactive marine bacterium Streptomyces albidoflavus VIP-1 from the Red Sea.BMC microbiology · 2025Article
- Stereoselective Conversions of Carbohydrate Anomeric Hydroxyl Group in Basic and Neutral Conditions.Molecules (Basel, Switzerland) · 2024Review
- Characterization of Two Glycoside Hydrolases of Family GH13 and GH57, Present in a Polysaccharide Utilization Locus (PUL) ofMolecules (Basel, Switzerland) · 2024Article
- Architecture, Function, Regulation, and Evolution of α-Glucans Metabolic Enzymes in Prokaryotes.Chemical reviews · 2024Review
- Synthesis of CFrontiers in chemistry · 2022Article
- Stereoselective synthesis of a 4-⍺-glucoside of valienamine and its X-ray structure in complex with Streptomyces coelicolor GlgE1-V279S.Scientific reports · 2021Article
- Trehalose and α-glucan mediate distinct abiotic stress responses in Pseudomonas aeruginosa.PLoS genetics · 2021Article
- A temperature-sensitive Mycobacterium smegmatis glgE mutation leads to a loss of GlgE enzyme activity and thermostability and the accumulation of α-maltose-1-phosphate.Biochimica et biophysica acta. General subjects · 2021Article
- Geochemical and metagenomics study of a metal-rich, green-turquoise-coloured stream in the southern Swiss Alps.PloS one · 2021Article
- Promising Recent Strategies with Potential Clinical Translational Value to Combat Antibacterial Resistant Surge.Medicines (Basel, Switzerland) · 2019Review
- Article
- Zwitterionic pyrrolidene-phosphonates: inhibitors of the glycoside hydrolase-like phosphorylase Streptomyces coelicolor GlgEI-V279S.Organic & biomolecular chemistry · 2017Article
- Glycan Phosphorylases in Multi-Enzyme Synthetic Processes.Protein and peptide letters · 2017Review
- Ligand-bound Structures and Site-directed Mutagenesis Identify the Acceptor and Secondary Binding Sites of Streptomyces coelicolor Maltosyltransferase GlgE.The Journal of biological chemistry · 2016Article
- Metabolic Network for the Biosynthesis of Intra- and Extracellular α-Glucans Required for Virulence of Mycobacterium tuberculosis.PLoS pathogens · 2016Article
- Developmental delay in a Streptomyces venezuelae glgE null mutant is associated with the accumulation of α-maltose 1-phosphate.Microbiology (Reading, England) · 2016Article
- Structural Dissection of the Maltodextrin Disproportionation Cycle of the Arabidopsis Plastidial Disproportionating Enzyme 1 (DPE1).The Journal of biological chemistry · 2015Article
- Structure of Mycobacterium thermoresistibile GlgE defines novel conformational states that contribute to the catalytic mechanism.Scientific reports · 2015Article
- Crystal structures of Mycobacterium tuberculosis GlgE and complexes with non-covalent inhibitors.Scientific reports · 2015Article
- Synthesis of 2-deoxy-2,2-difluoro-α-maltosyl fluoride and its X-ray structure in complex with Streptomyces coelicolor GlgEI-V279S.Organic & biomolecular chemistry · 2015Article
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Authors and funding
10 authors at 2 institutions in 1 country.
Funding
Abstract
GlgE is a recently identified (1→4)-α-d-glucan:phosphate α-d-maltosyltransferase involved in α-glucan biosynthesis in bacteria and is a genetically validated anti-tuberculosis drug target. It is a member of the GH13_3 CAZy subfamily for which no structures were previously known. We have solved the structure of GlgE isoform I from Streptomyces coelicolor and shown that this enzyme has the same catalytic and very similar kinetic properties to GlgE from Mycobacterium tuberculosis. The S. coelicolor enzyme forms a homodimer with each subunit comprising five domains, including a core catalytic α-amylase-type domain A with a (β/α)(8) fold. This domain is elaborated with domain B and two inserts that are specifically configured to define a well conserved donor pocket capable of binding maltose. Domain A, together with domain N from the neighboring subunit, forms a hydrophobic patch that is close to the maltose-binding site and capable of binding cyclodextrins. Cyclodextrins competitively inhibit the binding of maltooligosaccharides to the S. coelicolor enzyme, showing that the hydrophobic patch overlaps with the acceptor binding site. This patch is incompletely conserved in the M. tuberculosis enzyme such that cyclodextrins do not inhibit this enzyme, despite acceptor length specificity being conserved. The crystal structure reveals two further domains, C and S, the latter being a helix bundle not previously reported in GH13 members. The structure provides a framework for understanding how GlgE functions and will help guide the development of inhibitors with therapeutic potential.
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