2CHO

Bacteroides thetaiotaomicron hexosaminidase with O-GlcNAcase activity

2CHO の概要

• エントリーDOI: 10.2210/pdb2cho/pdb
• 関連するPDBエントリー: 2CHN
• 分子名称: GLUCOSAMINIDASE, CALCIUM ION, ACETATE ION, ... (6 entities in total)
• 機能のキーワード: o-glcnacase, hydrolase, n-acetylglucosamine
• 由来する生物種: BACTEROIDES THETAIOTAOMICRON; 詳細
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 167475.64

構造登録者

Dennis, R.J.,Taylor, E.J.,Macauley, M.S.,Stubbs, K.A.,Turkenburg, J.P.,Hart, S.J.,Black, G.N.,Vocadlo, D.J.,Davies, G.J. (登録日: 2006-03-16, 公開日: 2006-06-19, 最終更新日: 2024-05-08)

主引用文献

Dennis, R.J.,Taylor, E.J.,Macauley, M.S.,Stubbs, K.A.,Turkenburg, J.P.,Hart, S.J.,Black, G.N.,Vocadlo, D.J.,Davies, G.J.
Structure and Mechanism of a Bacterial B-Glucosaminidase Having O-Glcnacase Activity
Nat.Struct.Mol.Biol., 13:365-, 2006

PubMed Abstract: O-GlcNAc is an abundant post-translational modification of serine and threonine residues of nucleocytoplasmic proteins. This modification, found only within higher eukaryotes, is a dynamic modification that is often reciprocal to phosphorylation. In a manner analogous to phosphatases, a glycoside hydrolase termed O-GlcNAcase cleaves O-GlcNAc from modified proteins. Enzymes with high sequence similarity to human O-GlcNAcase are also found in human pathogens and symbionts. We report the three-dimensional structure of O-GlcNAcase from the human gut symbiont Bacteroides thetaiotaomicron both in its native form and in complex with a mimic of the reaction intermediate. Mutagenesis and kinetics studies show that the bacterial enzyme, very similarly to its human counterpart, operates via an unusual 'substrate-assisted' catalytic mechanism, which will inform the rational design of enzyme inhibitors.

PubMed: 16565725
DOI: 10.1038/NSMB1079

実験手法

X-RAY DIFFRACTION (1.85 Å)