6i3b
From Proteopedia
(Difference between revisions)
| Line 3: | Line 3: | ||
<StructureSection load='6i3b' size='340' side='right'caption='[[6i3b]], [[Resolution|resolution]] 1.00Å' scene=''> | <StructureSection load='6i3b' size='340' side='right'caption='[[6i3b]], [[Resolution|resolution]] 1.00Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
| - | <table><tr><td colspan='2'>[[6i3b]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6I3B OCA]. For a <b>guided tour on the structure components</b> use [http:// | + | <table><tr><td colspan='2'>[[6i3b]] is a 2 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=6I3B OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=6I3B FirstGlance]. <br> |
| - | </td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http:// | + | </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=6i3b FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6i3b OCA], [http://pdbe.org/6i3b PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6i3b RCSB], [http://www.ebi.ac.uk/pdbsum/6i3b PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6i3b ProSAT]</span></td></tr> |
</table> | </table> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == 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<ref>PMID:33006397</ref> | ||
| + | |||
| + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| + | </div> | ||
| + | <div class="pdbe-citations 6i3b" style="background-color:#fffaf0;"></div> | ||
| + | == References == | ||
| + | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
| + | [[Category: Synthetic construct sequences]] | ||
[[Category: Deridder, E]] | [[Category: Deridder, E]] | ||
[[Category: Mylemans, B]] | [[Category: Mylemans, B]] | ||
Current revision
Crystal structure of cPizza6-AYW, a circularly permuted designer protein
| |||||||||||
