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Crystal structures of a yeast 14‐3‐3 protein from Lachancea thermotolerans in the unliganded form and bound to a human lipid kinase PI4KB‐derived peptide reveal high evolutionary conservation
Author(s) -
Eisenreichova Andrea,
Klima Martin,
Boura Evzen
Publication year - 2016
Publication title -
acta crystallographica section f
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.572
H-Index - 37
ISSN - 2053-230X
DOI - 10.1107/s2053230x16015053
Subject(s) - biology , conserved sequence , biochemistry , phosphopeptide , yeast , microbiology and biotechnology , kinase , peptide sequence , gene
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.