Crystal Structure of β-Helical Antifreeze Protein Points to a General Ice Binding Model
pmid: 12015145
Crystal Structure of β-Helical Antifreeze Protein Points to a General Ice Binding Model
Reported here is the 2.3 A resolution crystal structure of spruce budworm (Choristoneura fumiferana) antifreeze protein (CfAFP), solved by single anomalous scattering. The structure reveals an extremely regular left-handed beta-helical platform consisting of 15-amino acid loops with a repetitive Thr-X-Thr motif displayed on one of the helix's three faces. This motif results in a two-dimensional array of threonine residues in an identical orientation to those in the nonhomologous, right-handed beta-helical beetle AFP from Tenebrio molitor (TmAFP). The CfAFP structure led us to reevaluate our ice binding model, and the analysis of three possible modes of docking gives rise to a binding mechanism based on surface complementarity. This general mechanism is applicable to both fish and insect AFPs.
- Queen's University Canada
Models, Molecular, Threonine, Magnetic Resonance Spectroscopy, Molecular Structure, surface complementarity, Ice, Fishes, Hydrogen Bonding, Moths, single anomalous scattering, Crystallography, X-Ray, Protein Structure, Secondary, Structural Biology, Antifreeze Proteins, Animals, β helix, X-ray structure, ice binding, antifreeze protein, Molecular Biology, Dimerization, Protein Binding
Models, Molecular, Threonine, Magnetic Resonance Spectroscopy, Molecular Structure, surface complementarity, Ice, Fishes, Hydrogen Bonding, Moths, single anomalous scattering, Crystallography, X-Ray, Protein Structure, Secondary, Structural Biology, Antifreeze Proteins, Animals, β helix, X-ray structure, ice binding, antifreeze protein, Molecular Biology, Dimerization, Protein Binding
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