5UN9
The crystal structure of human O-GlcNAcase in complex with Thiamet-G
Summary for 5UN9
| Entry DOI | 10.2210/pdb5un9/pdb |
| Related | 5UN8 |
| Descriptor | Protein O-GlcNAcase, (3AR,5R,6S,7R,7AR)-2-(ETHYLAMINO)-5-(HYDROXYMETHYL)-5,6,7,7A-TETRAHYDRO-3AH-PYRANO[3,2-D][1,3]THIAZOLE-6,7-DIOL (3 entities in total) |
| Functional Keywords | human o-glcnacase, thiemat-g, hydrolase |
| Biological source | Homo sapiens (Human) |
| Cellular location | Isoform 3: Nucleus . Isoform 1: Cytoplasm : O60502 |
| Total number of polymer chains | 2 |
| Total formula weight | 116143.73 |
| Authors | |
| Primary citation | Li, B.,Li, H.,Lu, L.,Jiang, J. Structures of human O-GlcNAcase and its complexes reveal a new substrate recognition mode. Nat. Struct. Mol. Biol., 24:362-369, 2017 Cited by PubMed Abstract: Human O-GlcNAcase (hOGA) is the unique enzyme responsible for the hydrolysis of the O-linked β-N-acetyl glucosamine (O-GlcNAc) modification, an essential protein glycosylation event that modulates the function of numerous cellular proteins in response to nutrients and stress. Here we report crystal structures of a truncated hOGA, which comprises the catalytic and stalk domains, in apo form, in complex with an inhibitor, and in complex with a glycopeptide substrate. We found that hOGA forms an unusual arm-in-arm homodimer in which the catalytic domain of one monomer is covered by the stalk domain of the sister monomer to create a substrate-binding cleft. Notably, the residues on the cleft surface afford extensive interactions with the peptide substrate in a recognition mode that is distinct from that of its bacterial homologs. These structures represent the first model of eukaryotic enzymes in the glycoside hydrolase 84 (GH84) family and provide a crucial starting point for understanding the substrate specificity of hOGA, which regulates a broad range of biological and pathological processes. PubMed: 28319083DOI: 10.1038/nsmb.3390 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.5 Å) |
Structure validation
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