5VVV

Structural Investigations of the Substrate Specificity of Human O-GlcNAcase

5VVV の概要

• エントリーDOI: 10.2210/pdb5vvv/pdb
• 関連するPDBエントリー: 5VVO 5VVT 5VVU 5VVX
• 分子名称: Protein O-GlcNAcase, a-crystallin B, 2-acetamido-2-deoxy-beta-D-glucopyranose, ... (4 entities in total)
• 機能のキーワード: oga, human o-glcnacase, a-crystalline b, hydrolase
• 由来する生物種: Homo sapiens (Human); 詳細
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 119121.01

構造登録者

Li, B.,Jiang, J.,Li, H.,Hu, C.-W. (登録日: 2017-05-20, 公開日: 2017-09-27, 最終更新日: 2024-10-23)

主引用文献

Li, B.,Li, H.,Hu, C.W.,Jiang, J.
Structural insights into the substrate binding adaptability and specificity of human O-GlcNAcase.
Nat Commun, 8:666-666, 2017

PubMed Abstract: The O-linked β-N-acetyl glucosamine (O-GlcNAc) modification dynamically regulates the functions of numerous proteins. A single human enzyme O-linked β-N-acetyl glucosaminase (O-GlcNAcase or OGA) hydrolyzes this modification. To date, it remains largely unknown how OGA recognizes various substrates. Here we report the structures of OGA in complex with each of four distinct glycopeptide substrates that contain a single O-GlcNAc modification on a serine or threonine residue. Intriguingly, these glycopeptides bind in a bidirectional yet conserved conformation within the substrate-binding cleft of OGA. This study provides fundamental insights into a general principle that confers the substrate binding adaptability and specificity to OGA in O-GlcNAc regulation.O-linked β-N-acetyl glucosamine (O-GlcNAc) is an important protein modification that is hydrolyzed by O-GlcNAcase (OGA). Here the authors give insights into OGA substrate recognition by presenting four human OGA structures complexed with glycopeptide substrates containing a single O-GlcNAc modification on either a serine or threonine.

PubMed: 28939839
DOI: 10.1038/s41467-017-00865-1

実験手法

X-RAY DIFFRACTION (2.8 Å)