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| | <StructureSection load='6i3a' size='340' side='right'caption='[[6i3a]], [[Resolution|resolution]] 1.45Å' scene=''> | | <StructureSection load='6i3a' size='340' side='right'caption='[[6i3a]], [[Resolution|resolution]] 1.45Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[6i3a]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Synthetic_construct_sequences Synthetic construct sequences]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6I3A OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=6I3A FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[6i3a]] is a 1 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=6I3A OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6I3A FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=BR:BROMIDE+ION'>BR</scene></td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.45Å</td></tr> |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=6i3a FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6i3a OCA], [http://pdbe.org/6i3a PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6i3a RCSB], [http://www.ebi.ac.uk/pdbsum/6i3a PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6i3a ProSAT]</span></td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=BR:BROMIDE+ION'>BR</scene></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=6i3a FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6i3a OCA], [https://pdbe.org/6i3a PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6i3a RCSB], [https://www.ebi.ac.uk/pdbsum/6i3a PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6i3a ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
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| | </StructureSection> | | </StructureSection> |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Synthetic construct sequences]] | + | [[Category: Synthetic construct]] |
| - | [[Category: Deridder, E]] | + | [[Category: Deridder E]] |
| - | [[Category: Mylemans, B]] | + | [[Category: Mylemans B]] |
| - | [[Category: Noguchi, H]] | + | [[Category: Noguchi H]] |
| - | [[Category: Voet, A R.D]] | + | [[Category: Voet ARD]] |
| - | [[Category: Artificial protein]]
| + | |
| - | [[Category: Beta-propeller]]
| + | |
| - | [[Category: Circularly permuted designer protein]]
| + | |
| - | [[Category: De novo protein]]
| + | |
| - | [[Category: Pizza]]
| + | |
| Structural highlights
Publication Abstract from PubMed
The beta-propeller fold is adopted by a sequentially diverse family of repeat proteins with apparent rotational symmetry. While the structure is mostly stabilized by hydrophobic interactions, an additional stabilization is provided by hydrogen bonds between the N-and C-termini, which are almost invariably part of the same beta-sheet. This feature is often referred to as the "Velcro" closure. The positioning of the termini within a blade is variable and depends on the protein family. In order to investigate the influence of this location on protein structure, folding and stability, we created different circular permutants, and a circularized version, of the designer propeller protein named Pizza. This protein is perfectly symmetrical, possessing six identical repeats. While all mutants adopt the same structure, the proteins lacking the "Velcro" closure were found to be significantly less resistant to thermal and chemical denaturation. This could explain why such proteins are rarely observed in nature. Interestingly the most common "Velcro" configuration for this protein family was not the most stable among the Pizza variants tested. The circularized version shows dramatically improved stability, which could have implications for future applications.
Influence of circular permutations on the structure and stability of a six-fold circular symmetric designer protein.,Mylemans B, Noguchi H, Deridder E, Lescrinier E, Tame JRH, Voet ARD Protein Sci. 2020 Oct 2. doi: 10.1002/pro.3961. PMID:33006397[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Mylemans B, Noguchi H, Deridder E, Lescrinier E, Tame JRH, Voet ARD. Influence of circular permutations on the structure and stability of a six-fold circular symmetric designer protein. Protein Sci. 2020 Oct 2. doi: 10.1002/pro.3961. PMID:33006397 doi:http://dx.doi.org/10.1002/pro.3961
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