6qiz
From Proteopedia
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| - | '''Unreleased structure''' | ||
| - | + | ==CI-2, conformation 2== | |
| + | <StructureSection load='6qiz' size='340' side='right'caption='[[6qiz]], [[Resolution|resolution]] 1.65Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[6qiz]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6QIZ OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6QIZ FirstGlance]. <br> | ||
| + | </td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6qiz FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6qiz OCA], [http://pdbe.org/6qiz PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6qiz RCSB], [http://www.ebi.ac.uk/pdbsum/6qiz PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6qiz ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | == Function == | ||
| + | [[http://www.uniprot.org/uniprot/ICI2_HORVU ICI2_HORVU]] Inhibits both subtilisin and chymotrypsin. | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | The macromolecular machines of life use allosteric control to self-assemble, dissociate and change shape in response to signals. Despite enormous interest, the design of nanoscale allosteric assemblies has proven tremendously challenging. Here we present a proof of concept of allosteric assembly in which an engineered fold switch on the protein monomer triggers or blocks assembly. Our design is based on the hyper-stable, naturally monomeric protein CI2, a paradigm of simple two-state folding, and the toroidal arrangement with 6-fold symmetry that it only adopts in crystalline form. We engineer CI2 to enable a switch between the native and an alternate, latent fold that self-assembles onto hexagonal toroidal particles by exposing a favorable inter-monomer interface. The assembly is controlled on demand via the competing effects of temperature and a designed short peptide. These findings unveil a remarkable potential for structural metamorphosis in proteins and demonstrate key principles for engineering protein-based nanomachinery. | ||
| - | + | Engineering protein assemblies with allosteric control via monomer fold-switching.,Campos LA, Sharma R, Alvira S, Ruiz FM, Ibarra-Molero B, Sadqi M, Alfonso C, Rivas G, Sanchez-Ruiz JM, Romero Garrido A, Valpuesta JM, Munoz V Nat Commun. 2019 Dec 13;10(1):5703. doi: 10.1038/s41467-019-13686-1. PMID:31836707<ref>PMID:31836707</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | [[Category: | + | </div> |
| + | <div class="pdbe-citations 6qiz" style="background-color:#fffaf0;"></div> | ||
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Large Structures]] | ||
[[Category: Romero, A]] | [[Category: Romero, A]] | ||
| - | [[Category: Ruiz, F | + | [[Category: Ruiz, F M]] |
| + | [[Category: Chymotrypsin inhibitor 2]] | ||
| + | [[Category: Hydrolase inhibitor]] | ||
| + | [[Category: Plant protein]] | ||
Revision as of 09:14, 25 December 2019
CI-2, conformation 2
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