Molecular mechanisms of O-GlcNAcylation

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    Protein glycosylation with O-linked N-acetylglucosamine (OGlcNAc)
    is a reversible post-translational modification of serines/threonines on metazoan proteins and occurring with similar time scales, dynamics and stoichiometry as protein phosphorylation. Levels of this modification are regulated by two enzymes—O-GlcNAc transferase (OGT) and O-GlcNAc
    hydrolase (OGA). Although the biochemistry of these enzymes and functional implications of O-GlcNAc have been studied extensively, until recently the structures and molecular mechanisms of OGT/OGA were not understood. This review covers a body of recent work that has led to an understanding of the structure of OGA, its catalytic mechanism and the
    development of a plethora of different inhibitors that are finding their use in cell biological studies towards the functional implications of O-GlcNAc. Furthermore, the very recent structure determination of a bacterial OGT orthologue has given the first insights into the contribution of the tetratricopeptide repeats (TPRs) to the active site and the role
    of some residues in catalysis and substrate binding.
    Original languageEnglish
    Pages (from-to)551-557
    JournalCurrent Opinion in Structural Biology
    Issue number5
    Publication statusPublished - Oct 2008


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