2jlb

Xanthomonas campestris putative OGT (XCC0866), complex with UDP- GlcNAc phosphonate analogue

spinqualitylabelsall models 2jlb, resolution 2.50Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 2jlb is a 2 chain structure with sequence from Xanthomonas campestris pv. campestris. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 2.5Å Ligands: CL, MN, UDM Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function Q8PC69_XANCP Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMed Post-translational modification of protein serines/threonines with N-acetylglucosamine (O-GlcNAc) is dynamic, inducible and abundant, regulating many cellular processes by interfering with protein phosphorylation. O-GlcNAcylation is regulated by O-GlcNAc transferase (OGT) and O-GlcNAcase, both encoded by single, essential, genes in metazoan genomes. It is not understood how OGT recognises its sugar nucleotide donor and performs O-GlcNAc transfer onto proteins/peptides, and how the enzyme recognises specific cellular protein substrates. Here, we show, by X-ray crystallography and mutagenesis, that OGT adopts the (metal-independent) GT-B fold and binds a UDP-GlcNAc analogue at the bottom of a highly conserved putative peptide-binding groove, covered by a mobile loop. Strikingly, the tetratricopeptide repeats (TPRs) tightly interact with the active site to form a continuous 120 A putative interaction surface, whereas the previously predicted phosphatidylinositide-binding site locates to the opposite end of the catalytic domain. On the basis of the structure, we identify truncation/point mutants of the TPRs that have differential effects on activity towards proteins/peptides, giving first insights into how OGT may recognise its substrates. Structural insights into mechanism and specificity of O-GlcNAc transferase.,Clarke AJ, Hurtado-Guerrero R, Pathak S, Schuttelkopf AW, Borodkin V, Shepherd SM, Ibrahim AF, van Aalten DM EMBO J. 2008 Oct 22;27(20):2780-8. Epub 2008 Sep 25. PMID:18818698 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also O-GlcNAc transferase 3D structures

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