Thermal hysteresis protein YL-1

spinqualitylabelsall models Thermal hysteresis protein YL-1 (PDB code 1ezg) Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D

The beta sheet roll motif lines up the amino acid chain such that each turn interacts with a unit cell of the water ice crystal

Tenebrio molitor (Yellow mealworm beetle)

Contributes to protect body fluid from freezing at subzero temperatures. Lowers the freezing point of the hemolymph by about 2.5 degrees at a concentration of 1 mg/ml. Binds to nascent ice crystals and prevents further growth

Structural highlights

The beta-sheet roll motif sets up several lines of mostly the amino acid threonine which is able to hydrogen bond to water molecules and form a Ice-binding The beta-sheet roll is held together by Cysteine sulfur bridges which helps create the roll structure that allows this protein to position its amino acids in the manner shown.

References

Liou YC, Tocilj A, Davies PL, Jia Z. Mimicry of ice structure by surface hydroxyls and water of a beta-helix antifreeze protein. Nature. 2000 Jul 20;406(6793):322-4. doi: 10.1038/35018604. PMID: 10917536.

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