5UN8

Crystal Structure of human O-GlcNAcase in complex with glycopeptide p53

5UN8 の概要

• エントリーDOI: 10.2210/pdb5un8/pdb
• 関連するPDBエントリー: 5UN9
• 分子名称: Protein O-GlcNAcase, P53 peptide, 2-acetamido-2-deoxy-beta-D-glucopyranose, ... (4 entities in total)
• 機能のキーワード: human o-glcnacase; glycopeptide, hydrolase
• 由来する生物種: Homo sapiens (Human); 詳細
• タンパク質・核酸の鎖数: 8
• 化学式量合計: 236960.39

構造登録者

Li, B.,Jiang, J. (登録日: 2017-01-30, 公開日: 2017-03-15, 最終更新日: 2024-11-06)

主引用文献

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

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: 28319083
DOI: 10.1038/nsmb.3390

実験手法

X-RAY DIFFRACTION (2.13 Å)