8x0z
From Proteopedia
(Difference between revisions)
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| - | '''Unreleased structure''' | ||
| - | + | ==Crystal structure of A101C/A120C mutant of FfIBP== | |
| + | <StructureSection load='8x0z' size='340' side='right'caption='[[8x0z]], [[Resolution|resolution]] 2.10Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[8x0z]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Flavobacterium_frigoris_PS1 Flavobacterium frigoris PS1]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=8X0Z OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=8X0Z FirstGlance]. <br> | ||
| + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.1Å</td></tr> | ||
| + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=8x0z FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8x0z OCA], [https://pdbe.org/8x0z PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8x0z RCSB], [https://www.ebi.ac.uk/pdbsum/8x0z PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8x0z ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | 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. | ||
| - | + | Engineered ice-binding protein (FfIBP) shows increased stability and resistance to thermal and chemical denaturation compared to the wildtype.,Nam Y, Nguyen DL, Hoang T, Kim B, Lee JH, Do H Sci Rep. 2024 Feb 8;14(1):3234. doi: 10.1038/s41598-024-53864-w. PMID:38331970<ref>PMID:38331970</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | [[Category: | + | </div> |
| + | <div class="pdbe-citations 8x0z" style="background-color:#fffaf0;"></div> | ||
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Flavobacterium frigoris PS1]] | ||
| + | [[Category: Large Structures]] | ||
| + | [[Category: Do H]] | ||
| + | [[Category: Nam Y]] | ||
Current revision
Crystal structure of A101C/A120C mutant of FfIBP
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