The asymmetric unit comprises two RiAFP molecules juxtaposed with their ice-binding surfaces, however the protein is monomer in the solutio
Overall Structure
The crystallographic structure of RiAFP was defined recently[1]. It reveals a new β-solenoid architecture that forms of of remarkable regularity. The β-sheets lie on top of each other with the upper and lower strands parallel but in the opposite orientation. Two ends deviate from β helix regularity by forming . These capping structures help to prevent end-to-end associations that would spoil the solubility of RiAFP and lead to oligomerization and aggregation.
The three residues in β-strand 11 at the C terminus that are too bulky to be accommodated into the core may also contribute to the capping structure to prevent amyloid-like polymerization. RiAFP solenoid possesses compressed nature with average distance between the sheets of only 6 Å. In the core of RiAFP, the side chains within apposed β-strands from the two β-sheets are staggered, allowing the side chains to interdigitate and pack tightly against one another. Most of the in the core are from Ala, Ser and Thr. Those residues create a more compact fold that may contribute to the high stability and antifreeze activity of RiAFP. Within the core there are between Thr-Ser (65-55, 85-75, 132-124 respectively) and one between Cys4-Cys21, that contributes to stabilization of the whole structure. The β-turns in the structure contain mostly Gly or Pro residues.
Ice Binding Surface (IBS)
IBS of RiAFP contains five expanded TXTXTXT motifs within the top (blue) β–sheet. These motifs are remarkably regular, allowing any rows/columns of TXTXTXT motifs to be exactly superposed onto any other rows/columns. Threonine residuses are crucial for maintaining antifreeze activity. It was found in other AFPs that mutations of the Thrs within these motifs decrease the thermal hysteresis.
Function
Disease
Relevance
Structural highlights
