6ttj | pdb_00006ttj
Neutral invertase 2 from Arabidopsis thaliana
Structural highlights
FunctionCINV1_ARATH Cytosolic invertase that specifically cleaves sucrose into glucose and fructose and is involved in the regulation of multiple tissue development including primary root elongation, root hair growth, leaf and silique development, and floral transition. Is involved in osmotic stress-induced inhibition on lateral root growth by controlling the concentration of hexose in cells. May regulate sugar-mediated root development by controlling sucrose catabolism in root cells.[1] [2] [3] [4] Publication Abstract from PubMedThe 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-beta 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 alpha-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 A resolution. The hexameric AtNIN2 structure is highly similar to that of InvA, pointing to high evolutionary conservation of neutral invertases. Crystal structure of Arabidopsis thaliana neutral invertase 2.,Tarkowski LP, Tsirkone VG, Osipov EM, Beelen S, Lammens W, Vergauwen R, Van den Ende W, Strelkov SV Acta Crystallogr F Struct Biol Commun. 2020 Mar 1;76(Pt 3):152-157. doi:, 10.1107/S2053230X2000179X. Epub 2020 Mar 3. PMID:32134001[5] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
| ||||||||||||||||||
