research communications
14-3-3 proteins bind phosphorylated binding partners to regulate several of their properties, including enzymatic activity, stability and subcellular localization. Here, two crystal structures are presented: the crystal structures of the 14-3-3 protein (also known as Bmh1) from the yeast Lachancea thermotolerans in the unliganded form and bound to a phosphopeptide derived from human PI4KB (phosphatidylinositol 4-kinase B). The structures demonstrate the high evolutionary conservation of ligand recognition by 14-3-3 proteins. The structural analysis suggests that ligand recognition by 14-3-3 proteins evolved very early in the evolution of eukaryotes and remained conserved, underlying the importance of 14-3-3 proteins in physiology.
Keywords: 14-3-3 proteins; Bmh1; Bmh2; crystal structure; phosphopeptide; PI4KB; Lachancea thermotolerans.
Supporting information
PDB references: Lachancea thermotolerans 14-3-3 protein, apo, 5lho; bound to PI4KB-derived peptide, 5li5