8X1P

Crystal structure of G160C/S176C mutant of FfIBP

8X1P の概要

• エントリーDOI: 10.2210/pdb8x1p/pdb
• 分子名称: Ice-binding protein (2 entities in total)
• 機能のキーワード: ice-binding protein, flavobacterium frigoris ps1, ice recrystallization, thermal hysteresis, antifreeze protein
• 由来する生物種: Flavobacterium frigoris PS1
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 25793.08

構造登録者

Nam, Y.,Do, H. (登録日: 2023-11-08, 公開日: 2024-11-13, 最終更新日: 2024-11-20)

主引用文献

Nam, Y.,Nguyen, D.L.,Hoang, T.,Kim, B.,Lee, J.H.,Do, H.
Engineered ice-binding protein (FfIBP) shows increased stability and resistance to thermal and chemical denaturation compared to the wildtype.
Sci Rep, 14:3234-3234, 2024

PubMed Abstract: Many polar organisms produce antifreeze proteins (AFPs) and ice-binding proteins (IBPs) to protect themselves from ice formation. As IBPs protect cells and organisms, the potential of IBPs as natural or biological cryoprotective agents (CPAs) for the cryopreservation of animal cells, such as oocytes and sperm, has been explored to increase the recovery rate after freezing-thawing. However, only a few IBPs have shown success in cryopreservation, possibly because of the presence of protein denaturants, such as dimethyl sulfoxide, alcohols, or ethylene glycol, in freezing buffer conditions, rendering the IBPs inactive. Therefore, we investigated the thermal and chemical stability of FfIBP isolated from Antarctic bacteria to assess its suitability as a protein-based impermeable cryoprotectant. A molecular dynamics (MD) simulation identified and generated stability-enhanced mutants (FfIBP_CC1). The results indicated that FfIBP_CC1 displayed enhanced resistance to denaturation at elevated temperatures and chemical concentrations, compared to wildtype FfIBP, and was functional in known CPAs while retaining ice-binding properties. Given that FfIBP shares an overall structure similar to DUF3494 IBPs, which are recognized as the most widespread IBP family, these findings provide important structural information on thermal and chemical stability, which could potentially be applied to other DUF3494 IBPs for future protein engineering.

PubMed: 38331970
DOI: 10.1038/s41598-024-53864-w

実験手法

X-RAY DIFFRACTION (2 Å)