Brief Communication abstract
Nature Structural & Molecular Biology 15, 764 - 765 (2008)
Published online: 8 June 2008 | doi:10.1038/nsmb.1443
Structure of an O-GlcNAc transferase homolog provides insight into intracellular glycosylation
Carlos Martinez-Fleites1, Matthew S Macauley2, Yuan He1, David L Shen2, David J Vocadlo2 & Gideon J Davies1
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.
- Structural Biology Laboratory, Department of Chemistry, The University of York, Heslington, York YO10 5YW, UK.
- Department of Chemistry, Simon Fraser University, 8888 University Drive, Burnaby, British Columbia V5A 1S6, Canada.
Correspondence to: Gideon J Davies1 e-mail: davies@ysbl.york.ac.uk
Correspondence to: David J Vocadlo2 e-mail: dvocadlo@sfu.ca
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