8X0Z
Crystal structure of A101C/A120C mutant of FfIBP
Summary for 8X0Z
| Entry DOI | 10.2210/pdb8x0z/pdb |
| Descriptor | Ice-binding protein (2 entities in total) |
| Functional Keywords | ice-binding protein, flavobacterium frigoris ps1, ice recrystallization, thermal hysteresis, antifreeze protein |
| Biological source | Flavobacterium frigoris PS1 |
| Total number of polymer chains | 1 |
| Total formula weight | 25795.05 |
| Authors | |
| Primary citation | 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 Cited by 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: 38331970DOI: 10.1038/s41598-024-53864-w PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.1 Å) |
Structure validation
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