5djs | pdb_00005djs

Thermobaculum terrenum O-GlcNAc transferase mutant - K341M

spinqualitylabelsall models 5djs, resolution 2.80Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 5djs is a 4 chain structure with sequence from "thermobaculum_terrenum"_botero_et_al._2004 "thermobaculum terrenum" botero et al. 2004. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: UDP Gene: Tter_2822 ("Thermobaculum terrenum" Botero et al. 2004) Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Publication Abstract from PubMed Post-translational modification of proteins is a ubiquitous mechanism of signal transduction in all kingdoms of life. One such modification is addition of O-linked N-acetylglucosamine to serine or threonine residues, known as O-GlcNAcylation. This unusual type of glycosylation is thought to be restricted to nucleocytoplasmic proteins of eukaryotes and is mediated by a pair of O-GlcNAc transferase and O-GlcNAc hydrolase enzymes operating on a large number of substrate proteins. Protein O-GlcNAcylation is responsive to glucose and flux through the hexosamine biosynthetic pathway. Thus, a close relationship is thought to exist between the level of O-GlcNAc proteins within and the general metabolic state of the cell. While isolated apparent orthologues of these enzymes are present in bacterial genomes, their biological functions remain largely unexplored. It is possible that understanding the function of these proteins will allow development of reductionist models to uncover the principles of O-GlcNAc signalling. Here, we identify orthologues of both O-GlcNAc cycling enzymes in the genome of the thermophilic eubacterium Thermobaculum terrenum. The O-GlcNAcase and O-GlcNAc transferase are co-expressed and, like their mammalian orthologues, localise to the cytoplasm. The O-GlcNAcase orthologue possesses activity against O-GlcNAc proteins and model substrates. We describe crystal structures of both enzymes, including an O-GlcNAcase-peptide complex, showing conservation of active sites with the human orthologues. Although in vitro activity of the O-GlcNAc transferase could not be detected, treatment of T. terrenum with an O-GlcNAc transferase inhibitor led to inhibition of growth. T. terrenum may be the first example of a bacterium possessing a functional O-GlcNAc system. Evidence for a functional O-GlcNAc system in the thermophilic bacterium Thermobaculum terrenum.,Ostrowski A, Gundogdu M, Ferenbach AT, Lebedev AA, van Aalten DM J Biol Chem. 2015 Oct 21. pii: jbc.M115.689596. PMID:26491011 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also O-GlcNAc transferase 3D structures

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