2YDR
CpOGA D298N in complex with p53-derived O-GlcNAc peptide
Summary for 2YDR
| Entry DOI | 10.2210/pdb2ydr/pdb |
| Related | 1A1U 1AIE 1C26 1DT7 1GZH 1H26 1HS5 1JSP 1KZY 1MA3 1OLG 1OLH 1PES 1PET 1SAE 1SAF 1SAH 1SAJ 1SAK 1SAL 1TSR 1TUP 1UOL 1XQH 1YCQ 1YCR 1YCS 2AC0 2ADY 2AHI 2ATA 2B3G 2BIM 2BIN 2BIO 2BIP 2BIQ 2CBI 2CBJ 2FEJ 2FOJ 2FOO 2GS0 2H1L 2J0Z 2J10 2J11 2J1W 2J1X 2J1Y 2J1Z 2J20 2J21 2J62 2JH2 2V5C 2V5D 2VUK 2VUR 2WB5 2WGX 2X0U 2X0V 2X0W 2X0Y 2XPK 2XWR 2YBG 2YDQ 2YDS 3SAK |
| Descriptor | O-GLCNACASE NAGJ, CELLULAR TUMOR ANTIGEN P53, CADMIUM ION, ... (5 entities in total) |
| Functional Keywords | hydrolase-peptide complex, cell cycle, hydrolase/peptide |
| Biological source | CLOSTRIDIUM PERFRINGENS More |
| Cellular location | Cytoplasm. Isoform 1: Nucleus. Isoform 2: Nucleus. Isoform 3: Nucleus. Isoform 4: Nucleus. Isoform 7: Nucleus. Isoform 8: Nucleus. Isoform 9: Cytoplasm: P04637 |
| Total number of polymer chains | 2 |
| Total formula weight | 69570.92 |
| Authors | Schimpl, M.,Borodkin, V.S.,Gray, L.J.,van Aalten, D.M.F. (deposition date: 2011-03-24, release date: 2012-03-14, Last modification date: 2024-10-23) |
| Primary citation | Schimpl, M.,Borodkin, V.S.,Gray, L.J.,Van Aalten, D.M.F. Synergy of Peptide and Sugar in O-Glcnacase Substrate Recognition. Chem.Biol., 19:173-, 2012 Cited by PubMed Abstract: 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. PubMed: 22365600DOI: 10.1016/J.CHEMBIOL.2012.01.011 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.75 Å) |
Structure validation
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