1prx
From Proteopedia
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'''HORF6 A NOVEL HUMAN PEROXIDASE ENZYME''' | '''HORF6 A NOVEL HUMAN PEROXIDASE ENZYME''' | ||
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[[Category: Ryu, S E.]] | [[Category: Ryu, S E.]] | ||
[[Category: Yang, C H.]] | [[Category: Yang, C H.]] | ||
| - | [[Category: | + | [[Category: Antioxidant]] |
| - | [[Category: | + | [[Category: Cellular signaling]] |
| - | [[Category: | + | [[Category: Horf6]] |
| - | [[Category: | + | [[Category: Hydrogen peroxide]] |
| - | [[Category: | + | [[Category: Peroxiredoxin]] |
| - | [[Category: | + | [[Category: Redox regulation]] |
| - | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 05:25:00 2008'' | |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | |
Revision as of 02:25, 3 May 2008
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 Sat May 3 05:25:00 2008
