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![[Figure 7]](wa5066fig7mag.jpg)
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Figure 7
Comparison of ice-binding sites of FfIBP with other β-helical fold IBPs. (a) Ice-binding residues on the B face of FfIBP. The ice-binding site of FfIBP has a very high Thr and Asn residue content. (b) Ice-binding residues on the B face of LeIBP. The ice-binding site residues of LeIBP are more diverse compared with the FfIBP structure. (c) The ice-binding site of FfIBP contains an ice-binding motif (T-A/G-X-T/N), while MpAFP (from Marinomonas primoryensis) has a T-X-N motif and CfAFP (from Choristoneura fumiferana) and TmAFP (from Tenebrio molitor) use a T-X-T motif for ice binding. Only the first and last residues of the ice-binding motif are connected in rectangular boxes to compare the ice-binding areas with one another. Notably, FfIBP contains three ice-binding motifs (T-A/G-X-T/N) on the B face, while LeIBP does not have a recognizable ice-binding motif. O and N atoms are shown in red and blue, respectively. |
![[Figure 7]](wa5066fig7.jpg)
 | STRUCTURAL BIOLOGY |
ISSN: 2059-7983
