1UCF

The Crystal Structure of DJ-1, a Protein Related to Male Fertility and Parkinson's Disease

Summary for 1UCF

• Entry DOI: 10.2210/pdb1ucf/pdb
• Descriptor: RNA-binding protein regulatory subunit (2 entities in total)
• Functional Keywords: flavodoxin-like rossmann fold, rna binding protein
• Biological source: Homo sapiens (human)
• Cellular location: Cytoplasm: Q99497
• Total number of polymer chains: 2
• Total formula weight: 39834.10

Authors

Honbou, K.,Suzuki, N.N.,Horiuchi, M.,Niki, T.,Taira, T.,Ariga, H.,Inagaki, F. (deposition date: 2003-04-11, release date: 2003-08-19, Last modification date: 2023-12-27)

Primary citation

Honbou, K.,Suzuki, N.N.,Horiuchi, M.,Niki, T.,Taira, T.,Ariga, H.,Inagaki, F.
The Crystal Structure of DJ-1, a Protein Related to Male Fertility and Parkinson's Disease
J.BIOL.CHEM., 278:31380-31384, 2003

PubMed 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.

PubMed: 12796482
DOI: 10.1074/jbc.M305878200

Experimental method

X-RAY DIFFRACTION (1.95 Å)