Arctic yeast Leucosporidium sp. produces a glycosylated ice-binding protein (LeIBP) with a molecular mass of ∼25 kDa, which can lower the freezing point below the melting point once it binds to ice. LeIBP is a member of a large class of ice-binding proteins. Here you can see the crystal structure of glycosylated LeIBP at 2.4 A resolution. Structural analysis of the LeIBPs revealed a dimeric right-handed β-helix fold, which is composed of three parts: a large coiled structural domain, a long helix region (residues 96-115 form a long α-helix that packs along one face of the β-helix), and a C-terminal hydrophobic loop region. Although LeIBP has a common β-helical fold similar to that of canonical hyperactive antifreeze proteins, the ice-binding site is more complex and does not have a simple ice-binding motif (PDB code: 3UYV)
#molecularart ... #immolecular ... #icebinding ... #artic ... #yeast ... #antifreeze ... #Komagataella ... #Xray.... Rendered with @proteinimaging and finished with @corelphotopaint
#molecularart ... #immolecular ... #icebinding ... #artic ... #yeast ... #antifreeze ... #Komagataella ... #Xray.... Rendered with @proteinimaging and finished with @corelphotopaint
