ArticleThe Plant cell2013
Structure of the Arabidopsis glucan phosphatase like sex four2 reveals a unique mechanism for starch dephosphorylation.
Article in The Plant cell, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.
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21 citing papers in PubMed, 36 citations in OpenAlex.
- Solving the Insoluble: Regulation of α-Polyglucan Solubility and Functionality in Nature.Molecules (Basel, Switzerland) · 2026Review
- Mechanistic insights into substrate-targeting modification effects on interfacial kinetics of raw starch-degrading amylases.Applied and environmental microbiology · 2026Article
- A structural perspective on α-glucan catabolism in oxygenic phototrophs.The Plant journal : for cell and molecular biology · 2026Review
- Identification of Novel Inhibitors of Starch Excess 4 (SEX4).Life (Basel, Switzerland) · 2024Article
- The LIKE SEX FOUR 1-malate dehydrogenase complex functions as a scaffold to recruit β-amylase to promote starch degradation.The Plant cell · 2023Article
- LIKE SEX4 1 Acts as a β-Amylase-Binding Scaffold on Starch Granules during Starch Degradation.The Plant cell · 2019Article
- Brain Glycogen Structure and Its Associated Proteins: Past, Present and Future.Advances in neurobiology · 2019Review
- Identification and analysis of OsttaDSP, a phosphoglucan phosphatase from Ostreococcus tauri.PloS one · 2018Article
- Functional Roles of Starch Binding Domains and Surface Binding Sites in Enzymes Involved in Starch Biosynthesis.Frontiers in plant science · 2018Review
- Structural biology of glucan phosphatases from humans to plants.Current opinion in structural biology · 2016Review
- Unique carbohydrate binding platforms employed by the glucan phosphatases.Cellular and molecular life sciences : CMLS · 2016Review
- Structural mechanisms of plant glucan phosphatases in starch metabolism.The FEBS journal · 2016Review
- The Starch Granule-Associated Protein EARLY STARVATION1 Is Required for the Control of Starch Degradation in Arabidopsis thaliana Leaves.The Plant cell · 2016Article
- Structure and expression of phosphoglucan phosphatase genes of Like Sex Four1 and Like Sex Four2 in barley.Genetica · 2016Article
- Assessing the Biological Activity of the Glucan Phosphatase Laforin.Methods in molecular biology (Clifton, N.J.) · 2016Article
- Mechanistic Insights into Glucan Phosphatase Activity against Polyglucan Substrates.The Journal of biological chemistry · 2015Article
- Structural mechanism of laforin function in glycogen dephosphorylation and lafora disease.Molecular cell · 2015Article
- A conformational landscape for alginate secretion across the outer membrane of Pseudomonas aeruginosa.Acta crystallographica. Section D, Biological crystallography · 2014Article
- Phosphoglucan-bound structure of starch phosphatase Starch Excess4 reveals the mechanism for C6 specificity.Proceedings of the National Academy of Sciences of the United States of America · 2014Article
- Expression, purification and characterization of soluble red rooster laforin as a fusion protein in Escherichia coli.BMC biochemistry · 2014Article
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9 authors at 2 institutions in 2 countries.
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Abstract
Starch is a water-insoluble, Glc-based biopolymer that is used for energy storage and is synthesized and degraded in a diurnal manner in plant leaves. Reversible phosphorylation is the only known natural starch modification and is required for starch degradation in planta. Critical to starch energy release is the activity of glucan phosphatases; however, the structural basis of dephosphorylation by glucan phosphatases is unknown. Here, we describe the structure of the Arabidopsis thaliana starch glucan phosphatase like sex four2 (LSF2) both with and without phospho-glucan product bound at 2.3Å and 1.65Å, respectively. LSF2 binds maltohexaose-phosphate using an aromatic channel within an extended phosphatase active site and positions maltohexaose in a C3-specific orientation, which we show is critical for the specific glucan phosphatase activity of LSF2 toward native Arabidopsis starch. However, unlike other starch binding enzymes, LSF2 does not possess a carbohydrate binding module domain. Instead we identify two additional glucan binding sites located within the core LSF2 phosphatase domain. This structure is the first of a glucan-bound glucan phosphatase and provides new insights into the molecular basis of this agriculturally and industrially relevant enzyme family as well as the unique mechanism of LSF2 catalysis, substrate specificity, and interaction with starch granules.
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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.