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1prx
From Proteopedia
(New page: 200px<br /> <applet load="1prx" size="450" color="white" frame="true" align="right" spinBox="true" caption="1prx, resolution 2.0Å" /> '''HORF6 A NOVEL HUMAN ...) |
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| - | [[Image:1prx.gif|left|200px]]<br /> | + | [[Image:1prx.gif|left|200px]]<br /><applet load="1prx" size="350" color="white" frame="true" align="right" spinBox="true" |
| - | <applet load="1prx" size=" | + | |
caption="1prx, resolution 2.0Å" /> | caption="1prx, resolution 2.0Å" /> | ||
'''HORF6 A NOVEL HUMAN PEROXIDASE ENZYME'''<br /> | '''HORF6 A NOVEL HUMAN PEROXIDASE ENZYME'''<br /> | ||
==Overview== | ==Overview== | ||
| - | Hydrogen peroxide (H2O2) has been implicated recently as an intracellular | + | 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== | ==About this Structure== | ||
| - | 1PRX is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http:// | + | 1PRX is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1PRX OCA]. |
==Reference== | ==Reference== | ||
| Line 14: | Line 13: | ||
[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
| - | [[Category: Choi, H | + | [[Category: Choi, H J.]] |
| - | [[Category: Kang, S | + | [[Category: Kang, S W.]] |
| - | [[Category: Rhee, S | + | [[Category: Rhee, S G.]] |
| - | [[Category: Ryu, S | + | [[Category: Ryu, S E.]] |
| - | [[Category: Yang, C | + | [[Category: Yang, C H.]] |
[[Category: antioxidant]] | [[Category: antioxidant]] | ||
[[Category: cellular signaling]] | [[Category: cellular signaling]] | ||
| Line 26: | Line 25: | ||
[[Category: redox regulation]] | [[Category: redox regulation]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:31:54 2008'' |
Revision as of 12:31, 21 February 2008
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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 Thu Feb 21 14:31:54 2008
