Structure of human O-GlcNAc transferase and its complex with a peptide substrate

Michael B. Lazarus, Yunsun Nam, Jiaoyang Jiang, Piotr Sliz () and Suzanne Walker ()
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Michael B. Lazarus: Harvard University
Yunsun Nam: Harvard Medical School
Jiaoyang Jiang: Harvard Medical School
Piotr Sliz: Harvard Medical School
Suzanne Walker: Harvard Medical School

Nature, 2011, vol. 469, issue 7331, 564-567

Abstract: Structure of a nutrient sensor O-GlcNAc transferase (OGT) is an essential mammalian enzyme that acts as a nutrient sensor. It glycosylates proteins with O-linked β-N-acetylglucosamine (O-GlcNAc), and this regulates a variety of cellular signalling pathways. Suzanne Walker and colleagues present the crystal structure of human OGT as a binary complex with UDP and as a ternary complex with UDP and a peptide substrate. The structures show how OGT recognizes peptide sequences, and provide information on the mechanism of action of an enzyme that has been found in aberrant form in a number of human conditions including diabetes, cancer and Alzheimer's disease.

Date: 2011
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DOI: 10.1038/nature09638

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