Abstract
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; Lachancea thermotolerans; PI4KB; crystal structure; phosphopeptide.
MeSH terms
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1-Phosphatidylinositol 4-Kinase / chemistry*
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1-Phosphatidylinositol 4-Kinase / genetics
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1-Phosphatidylinositol 4-Kinase / metabolism
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14-3-3 Proteins / chemistry*
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14-3-3 Proteins / genetics
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14-3-3 Proteins / metabolism
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Amino Acid Sequence
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Binding Sites
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Cloning, Molecular
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Conserved Sequence
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Crystallography, X-Ray
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Escherichia coli / genetics
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Escherichia coli / metabolism
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Evolution, Molecular
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Fungal Proteins / chemistry*
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Fungal Proteins / genetics
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Fungal Proteins / metabolism
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Gene Expression
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Humans
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Ligands
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Models, Molecular
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Phosphoproteins / chemistry*
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Phosphoproteins / genetics
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Phosphoproteins / metabolism
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Plasmids / chemistry
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Plasmids / metabolism
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Protein Binding
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Protein Conformation, alpha-Helical
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Protein Isoforms / chemistry
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Protein Isoforms / genetics
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Protein Isoforms / metabolism
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Recombinant Proteins / chemistry
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Recombinant Proteins / genetics
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Recombinant Proteins / metabolism
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Saccharomycetales / chemistry*
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Saccharomycetales / metabolism
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Sequence Alignment
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Structural Homology, Protein
Substances
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14-3-3 Proteins
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Fungal Proteins
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Ligands
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Phosphoproteins
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Protein Isoforms
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Recombinant Proteins
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1-Phosphatidylinositol 4-Kinase