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1prx
From Proteopedia
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HORF6 A NOVEL HUMAN PEROXIDASE ENZYME
Overview
Hydrogen peroxide (H2O2) has been implicated recently as an intracellular, messenger that affects cellular processes including protein, phosphorylation, transcription and apoptosis. A set of novel peroxidases, named peroxiredoxins (Prx), regulate the intracellular concentration of, H2O2 by reducing it in the presence of an appropriate electron donor. The, crystal structure of a human Prx enzyme, hORF6, reveals that the protein, contains two discrete domains and forms a dimer. The N-terminal domain has, a thioredoxin fold and the C-terminal domain is used for dimerization. The, active site cysteine (Cys 47), which exists as cysteine-sulfenic acid in, the crystal, is located at the bottom of a relatively narrow pocket. The, positively charged environment surrounding Cys 47 accounts for the, peroxidase activity of the enzyme, which contains no redox cofactors.
About this Structure
1PRX is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.
Reference
Crystal structure of a novel human peroxidase enzyme at 2.0 A resolution., Choi HJ, Kang SW, Yang CH, Rhee SG, Ryu SE, Nat Struct Biol. 1998 May;5(5):400-6. PMID:9587003
Page seeded by OCA on Mon Nov 12 18:46:34 2007
