Peroxiredoxin: Difference between revisions

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Alexander Berchansky, Michal Harel, Joel L. Sussman

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-[[Image:1qq2.png|left|200px|thumb|Crystal Structure of Peroxiredoxin ([[1qq2]])]]
+<StructureSection load='1qq2' size='350' side='right' scene='43/433646/Cv/2' caption='Typical 2-cys peroxiredoxin dimer complex with Cl- ions [[1qq2]]'>
-{{STRUCTURE_1qq2|  PDB=1qq2  | SIZE=300| SCENE=Peroxiredoxin/Cv/1 |right|CAPTION=Peroxiredoxin [[1qq2]]}}
+== Function ==
+[[Peroxiredoxin]] (Prx) is an antioxidant enzyme.  In the Prxs the active-site Cys is oxidized to sulfenic acid hyper oxide forming a Cys-SOH intermediate.  A second Cys residue resolves the intermediate to a protein disulfide bond.  The Prxs are divided into 3 types according to their intermediate resolving mechanism: '''typical 2-Cysteine Prx''' in which the Cys-Cys bond is formed between two subunits, '''atypical 2-Cys Prx''' in which the bond is formed within one subunit and '''1-Cysteine Prx''' which uses a single Cys residue for the catalysis. '''Prx Q''' is the plant homolog of [[Bacterioferritin comigratory protein]].
-[[Peroxiredoxin]] (Prx) is an antioxidant enzyme.  In the Prxs the active-site Cys is oxidized to sulfenic acid byperoxide.  The Prxs are divided into typical 2-Cys Prx, atypical 2-Cys Prx and 1-Cys Prx. The images at the left and at the right correspond to one representative Prx, ''i.e.'' the crystal structure of Peroxiredoxin from rat ([[1qq2]]).
+'''Typical 2-Cys Prx'''<br />
+* '''Prx 1''' interacts with signaling molecules<ref>PMID:19923889</ref>.
+* '''Prx 2''' is essential for sustaining erythrocyte life span<ref>PMID:18479207</ref>.
+* '''Prx 3''' is mitochondria-specific.<ref>PMID:15280382</ref>.
+* '''Prx 4''' localizes to the cytoplasm and regulates the activation of NF-κB<ref>PMID:25656995</ref>.
+'''Atypical 2-Cys Prx'''<br />
+* '''Prx 5''' protects from mitochondrial DNA damage induced by H<sub>2</sub>O<sub>2</sub><ref>PMID:15848167</ref>.
+'''1-Cys Prx'''<br />
+* '''Prx 6''' reduces peroxidized membrane phospholipids<ref>PMID:20919932</ref>.
+== Relevance ==
+Prx are over expressed in cancer tissue<ref>PMID:11497302</ref>.  Prx 4 mediates osteoclast activation in cancer cells<ref>PMID:25779674</ref>.
+== Structural highlights ==
+In the typical 2-cysteine Prx the <scene name='43/433646/Cv/5'>Cys-Cys bond is formed between two subunits</scene><ref>PMID:10535922</ref>. <scene name='43/433646/Cv/6'>Cl coordination site</scene>. Water molecules is shown as red sphere.
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 == 3D Structures of Peroxiredoxin ==
+[[Peroxiredoxin 3D structures]]
-[[1qq2]] – 2Cys-Prx – rat<br />
+</StructureSection>
-[[2c0d]] – 2Cys-Prx – ''Plasmodium falciparum''<br />
-[[1urm]] – hPrx 5 (mutant) – human<br />
-[[2vl2]], [[2vl3]], [[2vl9]] – hPrx 5<br />
-[[3mng]] – hPrx 5+DTT<br />
-[[2av5]] – Prx dot5 C-termianl (mutant) -yeast<br />
+== References ==
+<references/>
 [[Category:Topic Page]]