Loading
PDBj
MenuPDBj@FacebookPDBj@X(formerly Twitter)PDBj@BlueSkyPDBj@YouTubewwPDB FoundationwwPDBDonate
RCSB PDBPDBeBMRBAdv. SearchSearch help

6TTJ

Neutral invertase 2 from Arabidopsis thaliana

Summary for 6TTJ
Entry DOI10.2210/pdb6ttj/pdb
DescriptorAlkaline/neutral invertase CINV1 (1 entity in total)
Functional Keywordsinvertase, carbohydrate, hydrolase
Biological sourceArabidopsis thaliana (thale cress)
Total number of polymer chains12
Total formula weight754983.66
Authors
Tsirkone, V.G.,Osipov, E.M.,Beelen, S.,Strelkov, S.V. (deposition date: 2019-12-27, release date: 2020-03-11, Last modification date: 2024-01-24)
Primary citationTarkowski, 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
Cited by
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
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (3.392 Å)
Structure validation

247947

PDB entries from 2026-01-21

PDB statisticsPDBj update infoContact PDBjnumon