The crystal structure of DJ-1, a protein related to male fertility and Parkinson's disease - PubMed (original) (raw)

. 2003 Aug 15;278(33):31380-4.

doi: 10.1074/jbc.M305878200. Epub 2003 Jun 8.

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• PMID: 12796482
• DOI: 10.1074/jbc.M305878200

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The crystal structure of DJ-1, a protein related to male fertility and Parkinson's disease

Kazuya Honbou et al. J Biol Chem. 2003.

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Abstract

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.

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