6TTJ

Neutral invertase 2 from Arabidopsis thaliana

6TTJ の概要

• エントリーDOI: 10.2210/pdb6ttj/pdb
• 分子名称: Alkaline/neutral invertase CINV1 (1 entity in total)
• 機能のキーワード: invertase, carbohydrate, hydrolase
• 由来する生物種: Arabidopsis thaliana (thale cress)
• タンパク質・核酸の鎖数: 12
• 化学式量合計: 754983.66

構造登録者

Tsirkone, V.G.,Osipov, E.M.,Beelen, S.,Strelkov, S.V. (登録日: 2019-12-27, 公開日: 2020-03-11, 最終更新日: 2024-01-24)

主引用文献

Tarkowski, L.P.,Tsirkone, V.G.,Osipov, E.M.,Beelen, S.,Lammens, W.,Vergauwen, R.,Van den Ende, W.,Strelkov, S.V.
Crystal structure of Arabidopsis thaliana neutral invertase 2.
Acta Crystallogr.,Sect.F, 76:152-157, 2020

PubMed Abstract: The metabolism of sucrose is of crucial importance for life on Earth. In plants, enzymes called invertases split sucrose into glucose and fructose, contributing to the regulation of metabolic fluxes. Invertases differ in their localization and pH optimum. Acidic invertases present in plant cell walls and vacuoles belong to glycoside hydrolase family 32 (GH32) and have an all-β structure. In contrast, neutral invertases are located in the cytosol and organelles such as chloroplasts and mitochondria. These poorly understood enzymes are classified into a separate GH100 family. Recent crystal structures of the closely related neutral invertases InvA and InvB from the cyanobacterium Anabaena revealed a predominantly α-helical fold with unique features compared with other sucrose-metabolizing enzymes. Here, a neutral invertase (AtNIN2) from the model plant Arabidopsis thaliana was heterologously expressed, purified and crystallized. As a result, the first neutral invertase structure from a higher plant has been obtained at 3.4 Å resolution. The hexameric AtNIN2 structure is highly similar to that of InvA, pointing to high evolutionary conservation of neutral invertases.

PubMed: 32134001
DOI: 10.1107/S2053230X2000179X

実験手法

X-RAY DIFFRACTION (3.392 Å)