5ZBM

Structure of glycolate oxidase containing FMN from Nicotiana benthamiana

5ZBM の概要

• エントリーDOI: 10.2210/pdb5zbm/pdb
• 分子名称: Glycolate oxidase, FLAVIN MONONUCLEOTIDE (3 entities in total)
• 機能のキーワード: enzyme kinetics, saxs, oligomerization, oxidoreductase
• 由来する生物種: Nicotiana benthamiana
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 82198.61

構造登録者

Chen, Z.,Liu, Y. (登録日: 2018-02-12, 公開日: 2018-12-26, 最終更新日: 2023-11-22)

主引用文献

Liu, Y.,Wu, W.,Chen, Z.
Structures of glycolate oxidase from Nicotiana benthamiana reveal a conserved pH sensor affecting the binding of FMN.
Biochem.Biophys.Res.Commun., 503:3050-3056, 2018

PubMed Abstract: Glycolate oxidase (GOX), a flavin mononucleotide (FMN)-dependent enzyme, modulates reactive oxygen species-mediated signal transduction in green plants. It has been a target protein for crop improvement because of performing a key step in photorespiration that causes the energy losses. In human, GOX is involved in the production of oxalate, which is a key metabolite in the formation of kidney stone. Here, we report the first apo-GOX structure and its complex structure with cofactor FMN from Nicotiana benthamiana by X-ray crystallography. The binding of FMN induces a pronounced conformational change of GOX tetramer. Interestingly, a conserved pH sensor found among different species might directly regulate the binding of FMN and the enzyme activity. Combined with enzymatic experiments and biophysical analyses, we provide new insights in the molecular mechanism of regulating GOX biological activity reversibly and new methods of agricultural production and clinical application.

PubMed: 30143257
DOI: 10.1016/j.bbrc.2018.08.092

実験手法

X-RAY DIFFRACTION (2.8 Å)