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4d73
From Proteopedia
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<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://www.rcsb.org/pdb/explore.do?structureId=4d73 RCSB], [http://www.ebi.ac.uk/pdbsum/4d73 PDBsum]</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://www.rcsb.org/pdb/explore.do?structureId=4d73 RCSB], [http://www.ebi.ac.uk/pdbsum/4d73 PDBsum]</span></td></tr> | ||
</table> | </table> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == 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<ref>PMID:25952724</ref> | ||
| + | |||
| + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| + | </div> | ||
| + | == References == | ||
| + | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
Revision as of 06:40, 20 May 2015
X-ray structure of a peroxiredoxin
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