3tjj

Crystal structure of human peroxiredoxin IV C245A mutant in sulfenylated form

spinqualitylabelsall models 3tjj, resolution 1.91Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 3tjj is a 5 chain structure with sequence from Homo sapiens. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 1.91Å Ligands: CSO Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function PRDX4_HUMAN Probably involved in redox regulation of the cell. Regulates the activation of NF-kappa-B in the cytosol by a modulation of I-kappa-B-alpha phosphorylation. Publication Abstract from PubMed Peroxiredoxin IV (PrxIV) is an endoplasmic reticulum (ER) localized enzyme that metabolizes the hydrogen peroxide produced by ER oxidase 1 (Ero1). It has been shown to play a role in de novo disulfide formation, oxidizing members of the protein disulfide isomerase (PDI) family of enzymes and is a member of the typical 2-cys peroxiredoxin family. We have determined the crystal structure of both reduced and disulfide-bonded, as well as a resolving cysteine mutant of human PrxIV. We show that PrxIV has a similar structure to other typical 2-cys peroxiredoxins and undergoes a conformational change from a fully folded (FF) to a locally unfolded (LU) form following the formation of a disulfide between the peroxidatic and resolving cysteine residues. Unlike other mammalian typical 2-cys peroxiredoxins, we show that PrxIV forms a stable decameric structure even in its disulfide bonded state. In addition, the structure of a resolving cysteine mutant reveals an intermediate in the reaction cycle that adopts the LU conformation. Interestingly the peroxidatic cysteine in the crystal structure is sulfenylated rather than sulfinylated or sulfonylated. In addition, the peroxidatic cysteine in the resolving cysteine mutant is resistant to hyper-oxidation following incubation with high concentration of hydrogen peroxide. These results highlight some unique properties of PrxIV and suggest that the equilibrium between the FF and LU forms favors the LU conformation upon sulfenylation of the peroxidatic cysteine residue. Crystal structure of reduced and of oxidized peroxiredoxin IV reveals a stable oxidized decamer and a non disulfide-bonded intermediate in the catalytic cycle.,Cao Z, Tavender TJ, Roszak AW, Cogdell RJ, Bulleid NJ J Biol Chem. 2011 Oct 12. PMID:21994946 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Peroxiredoxin 3D structures

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