Published in

Nature Research, Nature Structural and Molecular Biology, 7(15), p. 764-765, 2008

DOI: 10.1038/nsmb.1443

Links

Tools

Export citation

Search in Google Scholar

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

Journal article published in 2008 by Carlos Martinez-Fleites, Matthew S. Macauley, Yuan He, David L. Shen, David J. Vocadlo, Gideon J. Davies ORCID
This paper is made freely available by the publisher.
This paper is made freely available by the publisher.

Full text: Download

Green circle
Preprint: archiving allowed
Upload
Orange circle
Postprint: archiving restricted
Upload
Red circle
Published version: archiving forbidden
Policy details
Data provided by SHERPA/RoMEO

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.