ArticleActa crystallographica. Section F, Structural biology communications2020
Crystal structure of Arabidopsis thaliana neutral invertase 2.
Article in Acta crystallographica. Section F, Structural biology communications, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 papers.
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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4 citing papers in PubMed, 4 citations in OpenAlex.
- Discovery and structural analysis of glycoside hydrolase family 176 α-1,2 glucosidase from Arthrobacter humicola A8F5.The Journal of biological chemistry · 2026Article
- Oligomeric Structure of Yeast and Other Invertases Governs Specificity.Sub-cellular biochemistry · 2024Review
- Insights into the Structure of the Highly Glycosylated Ffase fromInternational journal of molecular sciences · 2022Article
- QTL Mapping and GWAS Reveal the Genetic Mechanism Controlling Soluble Solids Content inFoods (Basel, Switzerland) · 2021Article
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Authors and funding
8 authors at 2 institutions in 2 countries.
Funding
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.
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