Identification of the ice‐binding face of a plant antifreeze protein
Copyright policy )Identification of the ice‐binding face of a plant antifreeze protein
The antifreeze protein of Lolium perenne, a perennial ryegrass, was previously modeled as a beta‐roll with two extensive flat beta‐sheets on opposite sides of the molecule. Here we have validated the model with a series of nine site‐directed steric mutations in which outward‐pointing short side‐chain residues were replaced by tyrosine. None of these disrupted the fold. Mutations on one of the beta‐sheets and on the sides of the protein retained 70% or greater activity. Three mutations that clustered on the other flat surface lost up to 90% of their antifreeze activity and identify this beta‐sheet as the ice‐binding face.
- Queen's University Canada
- Queen's University Canada
- Queen's University (Ontario, Canada) Canada
Models, Molecular, Protein Folding, Surface Properties, Molecular Sequence Data, Circular dichroism, Protein Structure, Secondary, Antifreeze Proteins, Escherichia coli, Lolium, Amino Acid Sequence, Antifreeze protein, Plant Proteins, Binding Sites, Sequence Homology, Amino Acid, Reproducibility of Results, Plant, Mutagenesis, Mutation, Mutagenesis, Site-Directed, Thermal hysteresis, Tyrosine, Ryegrass, Hydrophobic and Hydrophilic Interactions, Protein Binding
Models, Molecular, Protein Folding, Surface Properties, Molecular Sequence Data, Circular dichroism, Protein Structure, Secondary, Antifreeze Proteins, Escherichia coli, Lolium, Amino Acid Sequence, Antifreeze protein, Plant Proteins, Binding Sites, Sequence Homology, Amino Acid, Reproducibility of Results, Plant, Mutagenesis, Mutation, Mutagenesis, Site-Directed, Thermal hysteresis, Tyrosine, Ryegrass, Hydrophobic and Hydrophilic Interactions, Protein Binding
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