7c87
From Proteopedia
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| - | '''Unreleased structure''' | ||
| - | + | ==Peroxiredoxin from Aeropyrum pernix K1 (ApPrx) C50S/F80C/C207S/C213S mutant (ApPrx*F80C)== | |
| + | <StructureSection load='7c87' size='340' side='right'caption='[[7c87]], [[Resolution|resolution]] 2.20Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[7c87]] is a 10 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=7C87 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7C87 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]] 2.2Å</td></tr> | ||
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CIT:CITRIC+ACID'>CIT</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=7c87 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7c87 OCA], [https://pdbe.org/7c87 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7c87 RCSB], [https://www.ebi.ac.uk/pdbsum/7c87 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7c87 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®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | [[Category: | + | </div> |
| - | [[Category: Himiyama | + | <div class="pdbe-citations 7c87" style="background-color:#fffaf0;"></div> |
| - | [[Category: Nakamura | + | |
| + | ==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]] | ||
Current revision
Peroxiredoxin from Aeropyrum pernix K1 (ApPrx) C50S/F80C/C207S/C213S mutant (ApPrx*F80C)
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