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| | <StructureSection load='4d73' size='340' side='right'caption='[[4d73]], [[Resolution|resolution]] 1.80Å' scene=''> | | <StructureSection load='4d73' size='340' side='right'caption='[[4d73]], [[Resolution|resolution]] 1.80Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[4d73]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Plafa Plafa]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4D73 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4D73 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[4d73]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Plasmodium_falciparum Plasmodium falciparum]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4D73 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4D73 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='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=4d73 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4d73 OCA], [https://pdbe.org/4d73 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4d73 RCSB], [https://www.ebi.ac.uk/pdbsum/4d73 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4d73 ProSAT]</span></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=4d73 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4d73 OCA], [http://pdbe.org/4d73 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4d73 RCSB], [http://www.ebi.ac.uk/pdbsum/4d73 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4d73 ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | + | == Function == |
| | + | [[https://www.uniprot.org/uniprot/Q5MYR6_PLAF7 Q5MYR6_PLAF7]] |
| | <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: Plasmodium falciparum]] |
| - | [[Category: Plafa]]
| + | [[Category: Buechler M]] |
| - | [[Category: Buechler, M]] | + | [[Category: Deponte M]] |
| - | [[Category: Deponte, M]] | + | [[Category: Djuika CF]] |
| - | [[Category: Djuika, C F]] | + | [[Category: Koduka J]] |
| - | [[Category: Koduka, J]] | + | [[Category: Kopp J]] |
| - | [[Category: Kopp, J]] | + | [[Category: Lanzer M]] |
| - | [[Category: Lanzer, M]] | + | [[Category: Schlossarek S]] |
| - | [[Category: Schlossarek, S]] | + | [[Category: Staudacher V]] |
| - | [[Category: Staudacher, V]] | + | |
| - | [[Category: Antioxidant protein]]
| + | |
| - | [[Category: Oxidoreductase]]
| + | |
| - | [[Category: Prx5]]
| + | |
| - | [[Category: Redox regulation]]
| + | |
| Structural highlights
Function
[Q5MYR6_PLAF7]
Publication Abstract from PubMed
Life under aerobic conditions has shaped peroxiredoxins (Prx) as ubiquitous thiol-dependent hydroperoxidases and redox-sensors. Structural features that balance the catalytically active or inactive redox states of Prx, and, therefore, their hydroperoxidase or sensor function, have so far been analyzed predominantly for Prx1-type enzymes. Here we identify and characterize two modulatory residues of the Prx5-type model enzyme PfAOP from the malaria parasite Plasmodium falciparum. Gain- and loss-of-function mutants reveal a correlation between the enzyme parameters as well as the inactivation susceptibility of PfAOP with the size of residue 109 and the presence or absence of a catalytically relevant but non-essential cysteine residue. Based on our kinetic data and the crystal structure of PfAOPL109M, we suggest a novel mechanism for balancing the hydroperoxidase activity and inactivation susceptibility of Prx5-type enzymes. Our study provides unexpected insights into Prx structure-function relationships and contributes to our understanding of what makes Prx good enzymes or redox-sensors.
Plasmodium falciparum antioxidant protein reveals a novel mechanism for balancing turnover and inactivation of peroxiredoxins.,Staudacher V, Djuika CF, Koduka J, Schlossarek S, Kopp J, Buchler M, Lanzer M, Deponte M Free Radic Biol Med. 2015 May 4. pii: S0891-5849(15)00193-8. doi:, 10.1016/j.freeradbiomed.2015.04.030. PMID:25952724[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Staudacher V, Djuika CF, Koduka J, Schlossarek S, Kopp J, Buchler M, Lanzer M, Deponte M. Plasmodium falciparum antioxidant protein reveals a novel mechanism for balancing turnover and inactivation of peroxiredoxins. Free Radic Biol Med. 2015 May 4. pii: S0891-5849(15)00193-8. doi:, 10.1016/j.freeradbiomed.2015.04.030. PMID:25952724 doi:http://dx.doi.org/10.1016/j.freeradbiomed.2015.04.030
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