8ek4
From Proteopedia
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| - | '''Unreleased structure''' | ||
| - | + | ==De novo designed ice-binding proteins from twist-constrained helices== | |
| + | <StructureSection load='8ek4' size='340' side='right'caption='[[8ek4]], [[Resolution|resolution]] 2.35Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[8ek4]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Synthetic_construct Synthetic construct]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=8EK4 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=8EK4 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]] 2.35Å</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=8ek4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8ek4 OCA], [https://pdbe.org/8ek4 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8ek4 RCSB], [https://www.ebi.ac.uk/pdbsum/8ek4 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8ek4 ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | 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. | ||
| - | + | De novo designed ice-binding proteins from twist-constrained helices.,de Haas RJ, Tas RP, van den Broek D, Zheng C, Nguyen H, Kang A, Bera AK, King NP, Voets IK, de Vries R Proc Natl Acad Sci U S A. 2023 Jul 4;120(27):e2220380120. doi: , 10.1073/pnas.2220380120. Epub 2023 Jun 26. PMID:37364125<ref>PMID:37364125</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | [[Category: | + | </div> |
| + | <div class="pdbe-citations 8ek4" style="background-color:#fffaf0;"></div> | ||
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Large Structures]] | ||
| + | [[Category: Synthetic construct]] | ||
| + | [[Category: Bera AK]] | ||
| + | [[Category: De Haas RJ]] | ||
Revision as of 07:19, 12 July 2023
De novo designed ice-binding proteins from twist-constrained helices
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