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InterPro: IPR019479 Peroxiredoxin, C-terminal

Protein matchesHelp
UniProtKB
Matches:
2644 proteins
AccessionHelp IPR019479 Peroxiredoxin_C
TypeHelp Domain
SignaturesHelp
InterPro RelationshipsHelp
Found in IPR012335 Thioredoxin fold
IPR012336 Thioredoxin-like fold
IPR017559 Peroxiredoxin
InterPro annotation
BioMart Logo Entry Details in BioMart
AbstractHelp

This entry represents the C-terminal domain of 1-Cys peroxiredoxin, a member of the peroxiredoxin superfamily which protect cells against membrane oxidation through glutathione (GSH)-dependent reduction of phospholipid hydroperoxides to corresponding alcohols [1]. The C-terminal domain is crucial for providing the extra cysteine necessary for dimerisation of the whole molecule. Loss of the enzyme's peroxidase activity is associated with oxidation of the catalytic cysteine found upstream of this domain. Glutathionylation, presumably through its disruption of protein structure, facilitates access for GSH, resulting in spontaneous reduction of the mixed disulphide to the sulphydryl and consequent activation of the enzyme [2]. The domain is associated with IPR000866, which carries the catalytic cysteine.

Structural linksHelp
SCOP: c.47.1.10
Database linksHelp
Enzyme: EC:1.11.1.15

Taxonomic coverageHelp

Overlapping InterPro entriesHelp
IPR019479 Numbers of overlapping proteins Average numbers of overlapping amino acids

Example proteinsHelp
O08709 Peroxiredoxin-6

P30041 Peroxiredoxin-6

P34227 Mitochondrial peroxiredoxin PRX1

Q21824 Probable peroxiredoxin prdx-3

Q9V3P0 Peroxiredoxin 1

More proteins


Example Proteins Key


InterPro entry accession number/name and structure databases Colour code
IPR017936 Thioredoxin-like
IPR000866 Alkyl hydroperoxide reductase/ Thiol specific antioxidant/ Mal allergen
IPR012335 Thioredoxin fold
IPR019479 Peroxiredoxin, C-terminal
IPR012336 Thioredoxin-like fold
SWISS-MODEL
PDB Chain
ModBase
CATH Domain
SCOP Domain

PublicationsHelp
1. Choi HJ, Kang SW, Yang CH, Rhee SG, Ryu SE.
Crystal structure of a novel human peroxidase enzyme at 2.0 A resolution.
Nat. Struct. Biol. 5 400-6 1998 [PubMed: 9587003]
http://dx.doi.org/10.1038/nsb0598-400
2. Manevich Y, Feinstein SI, Fisher AB.
Activation of the antioxidant enzyme 1-CYS peroxiredoxin requires glutathionylation mediated by heterodimerization with pi GST.
Proc. Natl. Acad. Sci. U.S.A. 101 3780-5 2004 [PubMed: 15004285]
http://dx.doi.org/10.1073/pnas.0400181101

Additional ReadingHelp
Smeets A, Loumaye E, Clippe A, Rees JF, Knoops B, Declercq JP.
The crystal structure of the C45S mutant of annelid Arenicola marina peroxiredoxin 6 supports its assignment to the mechanistically typical 2-Cys subfamily without any formation of toroid-shaped decamers.
Protein Sci. 17 2008 700-10 [PubMed: 18359859]
http://dx.doi.org/10.1110/ps.073399308
Nakamura T, Yamamoto T, Abe M, Matsumura H, Hagihara Y, Goto T, Yamaguchi T, Inoue T.
Oxidation of archaeal peroxiredoxin involves a hypervalent sulfur intermediate.
Proc. Natl. Acad. Sci. U.S.A. 105 2008 6238-42 [PubMed: 18436649]
http://dx.doi.org/10.1073/pnas.0709822105
Jonsson TJ, Johnson LC, Lowther WT.
Structure of the sulphiredoxin-peroxiredoxin complex reveals an essential repair embrace.
Nature 451 2008 98-101 [PubMed: 18172504]
http://dx.doi.org/10.1038/nature06415
Vedadi M, Lew J, Artz J, Amani M, Zhao Y, Dong A, Wasney GA, Gao M, Hills T, Brokx S, Qiu W, Sharma S, Diassiti A, Alam Z, Melone M, Mulichak A, Wernimont A, Bray J, Loppnau P, Plotnikova O, Newberry K, Sundararajan E, Houston S, Walker J, Tempel W, Bochkarev A, Kozieradzki I, Edwards A, Arrowsmith C, Roos D, Kain K, Hui R.
Genome-scale protein expression and structural biology of Plasmodium falciparum and related Apicomplexan organisms.
Mol. Biochem. Parasitol. 151 2007 100-10 [PubMed: 17125854]
http://dx.doi.org/10.1016/j.molbiopara.2006.10.011
Nakamura T, Yamamoto T, Inoue T, Matsumura H, Kobayashi A, Hagihara Y, Uegaki K, Ataka M, Kai Y, Ishikawa K.
Crystal structure of thioredoxin peroxidase from aerobic hyperthermophilic archaeon Aeropyrum pernix K1.
Proteins 62 2006 822-6 [PubMed: 16342268]
http://dx.doi.org/10.1002/prot.20796
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InterPro 24.0