Paper Citing NAMD - Abstract
Wilkens, Casper; Auger, Kyle D.; Anderson, Nolan T.; Meekins, David A.; Raththagala, Madushi; Abou Hachem, Maher; Payne, Christina M.; Gentry, Matthew S.; Svensson, Birte
Plant -glucan phosphatases SEX4 and LSF2 display different affinity for amylopectin and amylose
FEBS LETTERS, 590:118-128, JAN 2016
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 K-Dapp for amylopectin and amylose, and K-D for -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 -cyclodextrin. SEX4 has 50-fold lower K-Dapp 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.
