2YDQ: Cpoga D298n In Complex With Hoga-Derived O-Glcnac Peptide

Citation:
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.
PDB ID: 2YDQDownload
MMDB ID: 97894
PDB Deposition Date: 2011/3/24
Updated in MMDB: 2012/03
Experimental Method:
x-ray diffraction
Resolution: 2.6  Å
Source Organism:
Homo sapiens
Similar Structures:
Biological Unit for 2YDQ: dimeric; determined by author and by software (PISA)
Molecular Components in 2YDQ
Label Count Molecule
Proteins (2 molecules)
1
O-glcnacase Nagj(Gene symbol: CPF_RS07030)
Molecule annotation
1
Bifunctional Protein Ncoat(Gene symbol: OGA)
Molecule annotation
Chemicals (20 molecules)
1
1
2
19
* Click molecule labels to explore molecular sequence information.

Citing MMDB
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