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| | <StructureSection load='5xbq' size='340' side='right'caption='[[5xbq]], [[Resolution|resolution]] 2.25Å' scene=''> | | <StructureSection load='5xbq' size='340' side='right'caption='[[5xbq]], [[Resolution|resolution]] 2.25Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[5xbq]] is a 12 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5XBQ OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=5XBQ FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[5xbq]] is a 12 chain structure with sequence from [https://en.wikipedia.org/wiki/Pyrococcus_horikoshii_OT3 Pyrococcus horikoshii OT3]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5XBQ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5XBQ FirstGlance]. <br> |
| - | </td></tr><tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=OCS:CYSTEINESULFONIC+ACID'>OCS</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]] 2.25Å</td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[5xbr|5xbr]], [[5xbs|5xbs]]</td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=OCS:CYSTEINESULFONIC+ACID'>OCS</scene></td></tr> |
| - | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Peroxiredoxin Peroxiredoxin], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.11.1.15 1.11.1.15] </span></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=5xbq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5xbq OCA], [https://pdbe.org/5xbq PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5xbq RCSB], [https://www.ebi.ac.uk/pdbsum/5xbq PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5xbq ProSAT]</span></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=5xbq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5xbq OCA], [http://pdbe.org/5xbq PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5xbq RCSB], [http://www.ebi.ac.uk/pdbsum/5xbq PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5xbq ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/TDXH_PYRHO TDXH_PYRHO] |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | </StructureSection> | | </StructureSection> |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Peroxiredoxin]] | + | [[Category: Pyrococcus horikoshii OT3]] |
| - | [[Category: Nakamura, T]] | + | [[Category: Nakamura T]] |
| - | [[Category: Uegaki, K]] | + | [[Category: Uegaki K]] |
| - | [[Category: Dimer]]
| + | |
| - | [[Category: Dodecamer]]
| + | |
| - | [[Category: Oxidoreductase]]
| + | |
| Structural highlights
Function
TDXH_PYRHO
Publication Abstract from PubMed
Peroxiredoxin from Pyrococcus horikoshii (PhPrx) is a decameric protein formed by ring-type assembly of five dimers. To engineer the quaternary structure of PhPrx, we created a mutant PhPrx (PhPrx6m) by introducing six point mutations designed to dissociate PhPrx into dimers. Although PhPrx6m was a dimer in solution, the six dimers assembled into a dodecamer following crystallization. In the crystal structure, PhPrx6m was overoxidized, and the peroxidatic cysteine was in sulfonic acid form and two cysteines in the C-terminal region were linked by an intramolecular disulfide bond. Thus, we characterized the wild-type PhPrx overoxidized by hydrogen peroxide (PhPrxPer). Analytical ultracentrifugation showed that PhPrxPer had a higher molecular mass in solution than PhPrx. This was confirmed by analysis of the crystal structure of PhPrxPer, which was found to form a ring-type dodecamer composed of six dimers. The monomeric structures of PhPrx6m and PhPrxPer differed from that of PhPrx in the relative orientation of two domains, reflecting the number of dimers in the ring-type assembly. Unlike PhPrx, homologous peroxiredoxin from Aeropyrum pernix (ApPrx) did not undergo hexameric association. This property can be explained by the stronger connection between the two domains in ApPrx due to its C-terminal extension relative to PhPrx.
Alteration of molecular assembly of peroxiredoxins from hyperthermophilic archaea.,Nakamura T, Oshima M, Yasuda M, Shimamura A, Morita J, Uegaki K J Biochem. 2017 Dec 1;162(6):415-422. doi: 10.1093/jb/mvx045. PMID:28992240[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Nakamura T, Oshima M, Yasuda M, Shimamura A, Morita J, Uegaki K. Alteration of molecular assembly of peroxiredoxins from hyperthermophilic archaea. J Biochem. 2017 Dec 1;162(6):415-422. doi: 10.1093/jb/mvx045. PMID:28992240 doi:http://dx.doi.org/10.1093/jb/mvx045
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