BIOMAT Database Logo BIOMAT Database Logo

Structure of an O-GlcNAc transferase homolog provides insight into intracellular glycosylation. 2008

Carlos Martinez-Fleites, and Matthew S Macauley, and Yuan He, and David L Shen, and David J Vocadlo, and Gideon J Davies
Structural Biology Laboratory, Department of Chemistry, The University of York, Heslington, York YO10 5YW, UK.

N-Acetylglucosamine (O-GlcNAc) modification of proteins provides a mechanism for the control of diverse cellular processes through a dynamic interplay with phosphorylation. UDP-GlcNAc:polypeptidyl transferase (OGT) catalyzes O-GlcNAc addition. The structure of an intact OGT homolog and kinetic analysis of human OGT variants reveal a contiguous superhelical groove that directs substrates to the active site.

UI MeSH Term Description Entries
D007700 Kinetics The rate dynamics in chemical or physical systems.
D008958 Models, Molecular Models used experimentally or theoretically to study molecular shape, electronic properties, or interactions; includes analogous molecules, computer-generated graphics, and mechanical structures. Molecular Models,Model, Molecular,Molecular Model
D006031 Glycosylation The synthetic chemistry reaction or enzymatic reaction of adding carbohydrate or glycosyl groups. GLYCOSYLTRANSFERASES carry out the enzymatic glycosylation reactions. The spontaneous, non-enzymatic attachment of reducing sugars to free amino groups in proteins, lipids, or nucleic acids is called GLYCATION (see MAILLARD REACTION). Protein Glycosylation,Glycosylation, Protein
D006801 Humans Members of the species Homo sapiens. Homo sapiens,Man (Taxonomy),Human,Man, Modern,Modern Man
D001665 Binding Sites The parts of a macromolecule that directly participate in its specific combination with another molecule. Combining Site,Binding Site,Combining Sites,Site, Binding,Site, Combining,Sites, Binding,Sites, Combining
D013329 Structure-Activity Relationship The relationship between the chemical structure of a compound and its biological or pharmacological activity. Compounds are often classed together because they have structural characteristics in common including shape, size, stereochemical arrangement, and distribution of functional groups. Relationship, Structure-Activity,Relationships, Structure-Activity,Structure Activity Relationship,Structure-Activity Relationships
D014974 Xanthomonas A genus in the family XANTHOMONADACEAE whose cells produce a yellow pigment (Gr. xanthos - yellow). It is pathogenic to plants. Xanthomonas albilineans
D017351 N-Acetylglucosaminyltransferases Enzymes that catalyze the transfer of N-acetylglucosamine from a nucleoside diphosphate N-acetylglucosamine to an acceptor molecule which is frequently another carbohydrate. EC 2.4.1.-. N-Acetylglucosamine Transferases,N Acetylglucosamine Transferases,N Acetylglucosaminyltransferases,Transferases, N-Acetylglucosamine
D042541 Intracellular Space The area within CELLS. Subcellular Space,Intracellular Spaces,Space, Intracellular,Space, Subcellular,Spaces, Intracellular,Spaces, Subcellular,Subcellular Spaces
D050505 Mutant Proteins Proteins produced from GENES that have acquired MUTATIONS. Mutant Protein,Protein, Mutant,Proteins, Mutant

Related Publications

Carlos Martinez-Fleites, and Matthew S Macauley, and Yuan He, and David L Shen, and David J Vocadlo, and Gideon J Davies
Feedback Regulation of O-GlcNAc Transferase through Translation Control to Maintain Intracellular O-GlcNAc Homeostasis.
March 2021, International journal of molecular sciences,
Carlos Martinez-Fleites, and Matthew S Macauley, and Yuan He, and David L Shen, and David J Vocadlo, and Gideon J Davies
Substrate specificity provides insights into the sugar donor recognition mechanism of O-GlcNAc transferase (OGT).
January 2013, PloS one,
Carlos Martinez-Fleites, and Matthew S Macauley, and Yuan He, and David L Shen, and David J Vocadlo, and Gideon J Davies
Recognition of a glycosylation substrate by the O-GlcNAc transferase TPR repeats.
June 2017, Open biology,
Carlos Martinez-Fleites, and Matthew S Macauley, and Yuan He, and David L Shen, and David J Vocadlo, and Gideon J Davies
Structure of a novel O-linked N-acetyl-D-glucosamine (O-GlcNAc) transferase, GtfA, reveals insights into the glycosylation of pneumococcal serine-rich repeat adhesins.
July 2014, The Journal of biological chemistry,
Carlos Martinez-Fleites, and Matthew S Macauley, and Yuan He, and David L Shen, and David J Vocadlo, and Gideon J Davies
Structural insights into mechanism and specificity of O-GlcNAc transferase.
October 2008, The EMBO journal,
Carlos Martinez-Fleites, and Matthew S Macauley, and Yuan He, and David L Shen, and David J Vocadlo, and Gideon J Davies
Exploration of O-GlcNAc transferase glycosylation sites reveals a target sequence compositional bias.
May 2023, The Journal of biological chemistry,
Carlos Martinez-Fleites, and Matthew S Macauley, and Yuan He, and David L Shen, and David J Vocadlo, and Gideon J Davies
Structure-Based Evolution of Low Nanomolar O-GlcNAc Transferase Inhibitors.
October 2018, Journal of the American Chemical Society,
Carlos Martinez-Fleites, and Matthew S Macauley, and Yuan He, and David L Shen, and David J Vocadlo, and Gideon J Davies
X-inactivation normalizes O-GlcNAc transferase levels and generates an O-GlcNAc-depleted Barr body.
January 2014, Frontiers in genetics,
Carlos Martinez-Fleites, and Matthew S Macauley, and Yuan He, and David L Shen, and David J Vocadlo, and Gideon J Davies
Discovery of O-GlcNAc transferase inhibitors.
October 2005, Journal of the American Chemical Society,
Carlos Martinez-Fleites, and Matthew S Macauley, and Yuan He, and David L Shen, and David J Vocadlo, and Gideon J Davies
Structure of O-linked GlcNAc transferase: mediator of glycan-dependent signaling.
May 2000, Biochemical and biophysical research communications,
Copied contents to your clipboard!