1ucf
From Proteopedia
(New page: 200px<br /> <applet load="1ucf" size="450" color="white" frame="true" align="right" spinBox="true" caption="1ucf, resolution 1.95Å" /> '''The Crystal Structu...) |
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| - | [[Image:1ucf.gif|left|200px]]<br /> | + | [[Image:1ucf.gif|left|200px]]<br /><applet load="1ucf" size="350" color="white" frame="true" align="right" spinBox="true" |
| - | <applet load="1ucf" size=" | + | |
caption="1ucf, resolution 1.95Å" /> | caption="1ucf, resolution 1.95Å" /> | ||
'''The Crystal Structure of DJ-1, a Protein Related to Male Fertility and Parkinson's Disease'''<br /> | '''The Crystal Structure of DJ-1, a Protein Related to Male Fertility and Parkinson's Disease'''<br /> | ||
==Overview== | ==Overview== | ||
| - | DJ-1 is a multifunctional protein that plays essential roles in tissues | + | DJ-1 is a multifunctional protein that plays essential roles in tissues with higher order biological functions such as the testis and brain. DJ-1 is related to male fertility, and its level in sperm decreases in response to exposure to sperm toxicants. DJ-1 has also been identified as a hydroperoxide-responsive protein. Recently, a mutation of DJ-1 was found to be responsible for familial Parkinson's disease. Here, we present the crystal structure of DJ-1 refined to 1.95-A resolution. DJ-1 forms a dimer in the crystal, and the monomer takes a flavodoxin-like Rossmann-fold. DJ-1 is structurally most similar to the monomer subunit of protease I, the intracellular cysteine protease from Pyrococcus horikoshii, and belongs to the Class I glutamine amidotransferase-like superfamily. However, DJ-1 contains an additional alpha-helix at the C-terminal region, which blocks the putative catalytic site of DJ-1 and appears to regulate the enzymatic activity. DJ-1 may induce conformational changes to acquire catalytic activity in response to oxidative stress. |
==Disease== | ==Disease== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1UCF 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:// | + | 1UCF 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=1UCF OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Inagaki, F.]] | [[Category: Inagaki, F.]] | ||
[[Category: Niki, T.]] | [[Category: Niki, T.]] | ||
| - | [[Category: Suzuki, N | + | [[Category: Suzuki, N N.]] |
[[Category: Taira, T.]] | [[Category: Taira, T.]] | ||
[[Category: flavodoxin-like rossmann fold]] | [[Category: flavodoxin-like rossmann fold]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 15:22:57 2008'' |
Revision as of 13:23, 21 February 2008
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The Crystal Structure of DJ-1, a Protein Related to Male Fertility and Parkinson's Disease
Contents |
Overview
DJ-1 is a multifunctional protein that plays essential roles in tissues with higher order biological functions such as the testis and brain. DJ-1 is related to male fertility, and its level in sperm decreases in response to exposure to sperm toxicants. DJ-1 has also been identified as a hydroperoxide-responsive protein. Recently, a mutation of DJ-1 was found to be responsible for familial Parkinson's disease. Here, we present the crystal structure of DJ-1 refined to 1.95-A resolution. DJ-1 forms a dimer in the crystal, and the monomer takes a flavodoxin-like Rossmann-fold. DJ-1 is structurally most similar to the monomer subunit of protease I, the intracellular cysteine protease from Pyrococcus horikoshii, and belongs to the Class I glutamine amidotransferase-like superfamily. However, DJ-1 contains an additional alpha-helix at the C-terminal region, which blocks the putative catalytic site of DJ-1 and appears to regulate the enzymatic activity. DJ-1 may induce conformational changes to acquire catalytic activity in response to oxidative stress.
Disease
Known diseases associated with this structure: Amyotrophic lateral sclerosis-Parkinsonism/dementia complex 2 OMIM:[602533], Parkinson disease 7, autosomal recessive early-onset OMIM:[602533]
About this Structure
1UCF is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.
Reference
The crystal structure of DJ-1, a protein related to male fertility and Parkinson's disease., Honbou K, Suzuki NN, Horiuchi M, Niki T, Taira T, Ariga H, Inagaki F, J Biol Chem. 2003 Aug 15;278(33):31380-4. Epub 2003 Jun 8. PMID:12796482
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