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
Language English Country United States Media print-electronic
Document type Journal Article
PubMed
27827352
PubMed Central
PMC5101580
DOI
10.1107/s2053230x16015053
PII: S2053230X16015053
Knihovny.cz E-resources
- Keywords
- 14-3-3 proteins, Bmh1, Bmh2, Lachancea thermotolerans, PI4KB, crystal structure, phosphopeptide,
- MeSH
- 1-Phosphatidylinositol 4-Kinase chemistry genetics metabolism MeSH
- Escherichia coli genetics metabolism MeSH
- Gene Expression MeSH
- Phosphoproteins chemistry genetics metabolism MeSH
- Fungal Proteins chemistry genetics metabolism MeSH
- Cloning, Molecular MeSH
- Protein Conformation, alpha-Helical MeSH
- Conserved Sequence MeSH
- Crystallography, X-Ray MeSH
- Humans MeSH
- Ligands MeSH
- Evolution, Molecular MeSH
- Models, Molecular MeSH
- Plasmids chemistry metabolism MeSH
- Protein Isoforms chemistry genetics metabolism MeSH
- 14-3-3 Proteins chemistry genetics metabolism MeSH
- Recombinant Proteins chemistry genetics metabolism MeSH
- Saccharomycetales chemistry metabolism MeSH
- Amino Acid Sequence MeSH
- Sequence Alignment MeSH
- Structural Homology, Protein MeSH
- Protein Binding MeSH
- Binding Sites MeSH
- Check Tag
- Humans MeSH
- Publication type
- Journal Article MeSH
- Names of Substances
- 1-Phosphatidylinositol 4-Kinase MeSH
- Phosphoproteins MeSH
- Fungal Proteins MeSH
- Ligands MeSH
- Protein Isoforms MeSH
- 14-3-3 Proteins MeSH
- Recombinant Proteins MeSH
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.
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