View source for 7cqj


==Peroxiredoxin from Aeropyrum pernix K1 (ApPrx) C50S/K84A/C207S/C213S mutant (ApPrx*K84A)==
<StructureSection load='7cqj' size='340' side='right'caption='[[7cqj]], [[Resolution|resolution]] 2.90&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[7cqj]] is a 12 chain structure with sequence from [https://en.wikipedia.org/wiki/Aeropyrum_pernix_K1 Aeropyrum pernix K1]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7CQJ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7CQJ 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]] 2.9&#8491;</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=7cqj FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7cqj OCA], [https://pdbe.org/7cqj PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7cqj RCSB], [https://www.ebi.ac.uk/pdbsum/7cqj PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7cqj ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/TDXH_AERPE TDXH_AERPE] 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Direct control of the protein quaternary structure (QS) is challenging owing to the complexity of the protein structure. As a protein with a characteristic QS, peroxiredoxin from Aeropyrum pernix K1 (ApPrx) forms a decamer, wherein five dimers associate to form a ring. Here, we disrupted and reconstituted ApPrx QS via amino acid mutations and chemical modifications targeting hot spots for protein assembly. The decameric QS of an ApPrx* mutant, wherein all cysteine residues in wild-type ApPrx were mutated to serine, was destructed to dimers via an F80C mutation. The dimeric ApPrx*F80C mutant was then modified with a small molecule and successfully assembled as a decamer. Structural analysis confirmed that an artificially installed chemical moiety potentially facilitates suitable protein-protein interactions to rebuild a native structure. Rebuilding of dodecamer was also achieved through an additional amino acid mutation. This study describes a facile method to regulate the protein assembly state.

Rebuilding Ring-Type Assembly of Peroxiredoxin by Chemical Modification.,Himiyama T, Tsuchiya Y, Yonezawa Y, Nakamura T Bioconjug Chem. 2020 Dec 17. doi: 10.1021/acs.bioconjchem.0c00587. PMID:33334100<ref>PMID:33334100</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 7cqj" style="background-color:#fffaf0;"></div>

==See Also==
*[[Peroxiredoxin 3D structures|Peroxiredoxin 3D structures]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Aeropyrum pernix K1]]
[[Category: Large Structures]]
[[Category: Himiyama T]]
[[Category: Nakamura T]]