2ydq

CpOGA D298N in complex with hOGA-derived O-GlcNAc peptide

spinqualitylabelsall models 2ydq, resolution 2.60Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 2ydq is a 2 chain structure with sequence from Clostridium perfringens and Homo sapiens. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 2.6Å Ligands: CD, NAG Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function OGA_CLOP1 Biological function unknown. Capable of hydrolyzing the glycosidic link of O-GlcNAcylated proteins. Publication Abstract from PubMed Protein O-GlcNAcylation is an essential reversible posttranslational modification in higher eukaryotes. O-GlcNAc addition and removal is catalyzed by O-GlcNAc transferase and O-GlcNAcase, respectively. We report the molecular details of the interaction of a bacterial O-GlcNAcase homolog with three different synthetic glycopeptides derived from characterized O-GlcNAc sites in the human proteome. Strikingly, the peptides bind a conserved O-GlcNAcase substrate binding groove with similar orientation and conformation. In addition to extensive contacts with the sugar, O-GlcNAcase recognizes the peptide backbone through hydrophobic interactions and intramolecular hydrogen bonds, while avoiding interactions with the glycopeptide side chains. These findings elucidate the molecular basis of O-GlcNAcase substrate specificity, explaining how a single enzyme achieves cycling of the complete O-GlcNAc proteome. In addition, this work will aid development of O-GlcNAcase inhibitors that target the peptide binding site. Synergy of Peptide and Sugar in O-GlcNAcase Substrate Recognition.,Schimpl M, Borodkin VS, Gray LJ, van Aalten DM Chem Biol. 2012 Feb 24;19(2):173-8. PMID:22365600 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also O-GlcNAcase

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