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

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 analy...

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Veröffentlicht in:	Nature structural & molecular biology 2008-07, Vol.15 (7), p.764-765
Hauptverfasser:	Vocadlo, David J, Davies, Gideon J, Martinez-Fleites, Carlos, Macauley, Matthew S, He, Yuan, Shen, David L
Format:	Artikel
Sprache:	eng
Schlagworte:	Binding Sites Biochemistry Biological Microscopy Biomedical and Life Sciences brief-communication Catalysis Cellular signal transduction Glycosylation Humans Intracellular Space - metabolism Kinetics Life Sciences Membrane Biology Models, Molecular Molecular biology Molecular structure Mutant Proteins - metabolism N-Acetylglucosaminyltransferases - chemistry Phosphorylation Physiological aspects Protein Structure Proteins Structural Homology, Protein Structure-Activity Relationship Xanthomonas - enzymology
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Beschreibung
Zusammenfassung:	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.
ISSN:	1545-9993 1545-9985
DOI:	10.1038/nsmb.1443