Sandbox Reserved 381: Difference between revisions

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== ''O-GlcNAc transferase'' ==
== ''O-GlcNAc transferase'' ==


O-linked β-N-acetylglucosamine transferase (O-GlcNAc transferase) is an essential mammalian enzyme that acts as a nutrient sensor, coupling metabolic status to the regulation of a wide variety of cellular signaling pathways.<ref> Hart GW, Housley MP, Slawson C. Cycling of O-linked β-N-acetylglucosamine on nucleocytoplasmic proteins. Nature.2007;446:1017-22.[http://www.nature.com/nature/journal/v446/n7139/abs/nature05815.html]</ref> OGT catalyses the transfer of N-acetylglucosamine from UDP-N-acetylglucosamine (UDP-GlcNAc) to serines and threonines of cytoplasmic, nuclear and mitochondrial proteins, including numerous transcription factors, tumour suppressors, kinases, phospahateses and histone-modifying proteins.<ref>PMID:21240259</ref> Two crystal structures of human OGT are reported here, as a binary complex with UDP (2.8 A resolution) and as a ternary complex with UDP and a peptide substrate (1.95 A).
O-linked β-N-acetylglucosamine transferase (O-GlcNAc transferase) is an essential mammalian enzyme that acts as a nutrient sensor, coupling metabolic status to the regulation of a wide variety of cellular signaling pathways.<ref> Hart GW, Housley MP, Slawson C. Cycling of O-linked β-N-acetylglucosamine on nucleocytoplasmic proteins. Nature.2007;446:1017-22.[http://www.nature.com/nature/journal/v446/n7139/abs/nature05815.html]</ref> OGT catalyses the transfer of N-acetylglucosamine from UDP-N-acetylglucosamine (UDP-GlcNAc) to serines and threonines of cytoplasmic, nuclear and mitochondrial proteins, including numerous transcription factors, tumour suppressors, kinases, phospahateses and histone-modifying proteins.<ref>PMID:21240259</ref> The crystal structure of human OGT is reported here as a ternary complex with UDP and a peptide substrate.


== O-GlcNAc transferase Function ==
== O-GlcNAc transferase Function ==