Plant α-glucan phosphatases SEX4 and LSF2 display different affinity for amylopectin and amylose

FEBS Letters
Casper WilkensBirte Svensson

Abstract

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.

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Citations

May 6, 2016·Cellular and Molecular Life Sciences : CMLS·Shane EmanuelleMatthew S Gentry
Feb 23, 2020·Annual Review of Plant Biology·Alison M Smith, Samuel C Zeeman
Nov 30, 2018·Frontiers in Plant Science·Casper WilkensMarie Sofie Møller
Dec 27, 2019·Archives of Biochemistry and Biophysics·Julieta B CarrilloMariana Martín
Oct 7, 2018·Analytical Biochemistry·Savita SharmaCraig W Vander Kooi
Mar 5, 2021·Archives of Biochemistry and Biophysics·Yousra El MannaiEiji Suzuki
Aug 9, 2016·Current Opinion in Structural Biology·Matthew S GentryCraig W Vander Kooi

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