Plant α‐glucan phosphatases SEX4 and LSF2 display different affinity for amylopectin and amylose
Copyright policy )Plant α‐glucan phosphatases SEX4 and LSF2 display different affinity for amylopectin and amylose
The plant glucan phosphatases Starch EXcess 4 (SEX4) and Like Sex Four2 (LSF2) apply different starch binding mechanisms. SEX4 contains a carbohydrate binding module, and LSF2 has two surface binding sites (SBSs). We determined KDapp for amylopectin and amylose, and KD for β‐cyclodextrin and validated binding site mutants deploying affinity gel electrophoresis (AGE) and surface plasmon resonance. SEX4 has a higher affinity for amylopectin; LSF2 prefers amylose and β‐cyclodextrin. SEX4 has 50‐fold lower KDapp for amylopectin compared to LSF2. Molecular dynamics simulations and AGE data both support long‐distance mutual effects of binding at SBSs and the active site in LSF2.
- Technical University of Denmark Denmark
- University of Kentucky United States
Models, Molecular, Binding Sites, Arabidopsis Proteins, Protein Conformation, Amylopectin, beta-Cyclodextrins, Arabidopsis, Molecular Dynamics Simulation, Surface Plasmon Resonance, Cytoplasmic Granules, Recombinant Proteins, Substrate Specificity, Plant Leaves, Kinetics, Amino Acid Substitution, Mutation, Carbohydrate Conformation, Dual-Specificity Phosphatases, Amylose
Models, Molecular, Binding Sites, Arabidopsis Proteins, Protein Conformation, Amylopectin, beta-Cyclodextrins, Arabidopsis, Molecular Dynamics Simulation, Surface Plasmon Resonance, Cytoplasmic Granules, Recombinant Proteins, Substrate Specificity, Plant Leaves, Kinetics, Amino Acid Substitution, Mutation, Carbohydrate Conformation, Dual-Specificity Phosphatases, Amylose
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