8EK4

De novo designed ice-binding proteins from twist-constrained helices

8EK4 の概要

• エントリーDOI: 10.2210/pdb8ek4/pdb
• 分子名称: Ice-binding protein TIP-99a (1 entity in total)
• 機能のキーワード: de novo designed, ice-binding proteins, de novo protein
• 由来する生物種: synthetic construct
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 33191.75

構造登録者

Bera, A.K.,De Haas, R.J. (登録日: 2022-09-19, 公開日: 2023-07-12, 最終更新日: 2024-04-03)

主引用文献

de Haas, R.J.,Tas, R.P.,van den Broek, D.,Zheng, C.,Nguyen, H.,Kang, A.,Bera, A.K.,King, N.P.,Voets, I.K.,de Vries, R.
De novo designed ice-binding proteins from twist-constrained helices.
Proc.Natl.Acad.Sci.USA, 120:e2220380120-e2220380120, 2023

PubMed Abstract: Attaining molecular-level control over solidification processes is a crucial aspect of materials science. To control ice formation, organisms have evolved bewildering arrays of ice-binding proteins (IBPs), but these have poorly understood structure-activity relationships. We propose that reverse engineering using de novo computational protein design can shed light on structure-activity relationships of IBPs. We hypothesized that the model alpha-helical winter flounder antifreeze protein uses an unusual undertwisting of its alpha-helix to align its putative ice-binding threonine residues in exactly the same direction. We test this hypothesis by designing a series of straight three-helix bundles with an ice-binding helix projecting threonines and two supporting helices constraining the twist of the ice-binding helix. Our findings show that ice-recrystallization inhibition by the designed proteins increases with the degree of designed undertwisting, thus validating our hypothesis, and opening up avenues for the computational design of IBPs.

PubMed: 37364125
DOI: 10.1073/pnas.2220380120

実験手法

X-RAY DIFFRACTION (2.35 Å)