Identification of a novel ATPase activity in 14‐3‐3 proteins – Evidence from enzyme kinetics, structure guided modeling and mutagenesis studies
Copyright policy )Identification of a novel ATPase activity in 14‐3‐3 proteins – Evidence from enzyme kinetics, structure guided modeling and mutagenesis studies
14‐3‐3 Proteins bind phosphorylated sequences in proteins and regulate multiple cellular functions. For the first time, we show that pure recombinant human 14‐3‐3 ζ, γ, ε and τ isofoms hydrolyze ATP with similar K m and k cat values. In sharp contrast the sigma isoform has no detectable activity. Docking studies identify two putative binding pockets in 14‐3‐3 zeta. Mutation of D124A in the amphipathic pocket enhances binding affinity and catalysis. Mutation of a critical Arg (R55A) at the dimer interface in zeta reduces binding and decreases catalysis. These experimental results coincide with a binding pose at the dimer interface. This newly identified function could be a moon lighting function in some of these isoforms.
Models, Molecular, Blotting, Western, Molecular Sequence Data, Chaperone, Molecular Dynamics Simulation, Docking, Adenosine Triphosphate, Humans, Amino Acid Sequence, 14-3-3, Adenosine Triphosphatases, Binding Sites, Molecular Structure, Sequence Homology, Amino Acid, Hydrolysis, Recombinant Proteins, Protein Structure, Tertiary, Kinetics, 14-3-3 Proteins, Mutagenesis, ATP hydrolysis, Mutation, Protein Binding
Models, Molecular, Blotting, Western, Molecular Sequence Data, Chaperone, Molecular Dynamics Simulation, Docking, Adenosine Triphosphate, Humans, Amino Acid Sequence, 14-3-3, Adenosine Triphosphatases, Binding Sites, Molecular Structure, Sequence Homology, Amino Acid, Hydrolysis, Recombinant Proteins, Protein Structure, Tertiary, Kinetics, 14-3-3 Proteins, Mutagenesis, ATP hydrolysis, Mutation, Protein Binding
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