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Nat Struct Mol Biol. 2008 Jul;15(7):764-5. doi: 10.1038/nsmb.1443. Epub 2008 Jun 8.

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

Author information

1
Structural Biology Laboratory, Department of Chemistry, The University of York, Heslington, York YO10 5YW, UK.

Abstract

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.

PMID:
18536723
DOI:
10.1038/nsmb.1443
[Indexed for MEDLINE]

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