1. ZvAFP13 had certain thermal hysteresis (TH) activity, with a TH of 0.38 ± 0.03℃ at 1mg/ml and 0.96 ± 0.01℃ at 5mg/ml; ZvAFP6 was inactive on its own but nearly doubled the activity when combined with ZvAFP13.
2. The high-quality crystal structures of ZvAFP13 and ZvAFP6 were obtained. ZvAFP13 crystallized isomorphously to many other reported type III AFPs, while ZvAFP6 crystallized in the space group C2221 with two molecules in the asymmetric unit forming a dimer. This is the first report of dimerization of type III AFPs.
3. The overall folds of ZvAFP13 and ZvAFP6 are very similar, both being compact, globular single domains, but there are differences in certain regions. For example, some residues at the N- and C-termini of ZvAFP6 are disordered. No obvious difference was found in the water structure organization near the ice-binding site (IBS) of the two proteins, although previous studies have shown that the water structure in this region is important for AFP binding to ice.
AFP013010
General Information
| Protein Name | Ice-structuring protein |
| UniProt ID | R9S083 |
| Nucleotide Sequence ID in NCBI | KC622345.1 |
| Protein Sequence ID in NCBI | AGM97733.1 |
| Species | Zoarces viviparus (Viviparous eelpout) (Blennius viviparus) |
| Sequence Length | 66 |
| Sequence | |
| Structure | PDB ID: 4ur6 |
| Solvent Accessible Surface Area | Total SASA | 4218.66 Ų | Polar SASA | 2458.38 Ų | Apolar SASA | 6677.04 Ų |
AFP013010000
| Mutation | Wild Type |
| Sequence |
Thermal Hysteresis
| PMID | 25025819 |
| DOI | 10.1016/j.cryobiol.2014.07.003 |
| Protein Name | ZvAFP6 |
| Thermal Hysteresis | "The SP isoform ZvAFP6 was completely inactive on its own up to a concentration of 10 mg/ml." |
Brief description
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PMID: 25025819
DOI: 10.1016/j.cryobiol.2014.07.003 |