3BWE

Crystal structure of aggregated form of DJ1

Summary for 3BWE

• Entry DOI: 10.2210/pdb3bwe/pdb
• Descriptor: Protein DJ-1, PHOSPHATE ION (3 entities in total)
• Functional Keywords: dj-1, filamentous aggregates, chaperone, cytoplasm, disease mutation, nucleus, oncogene, oxidation, parkinson disease, phosphoprotein, polymorphism, ubl conjugation
• Biological source: Homo sapiens (Human)
• Cellular location: Cytoplasm: Q99497
• Total number of polymer chains: 7
• Total formula weight: 141725.47

Authors

Cha, S.S. (deposition date: 2008-01-09, release date: 2008-10-14, Last modification date: 2024-11-06)

Primary citation

Cha, S.S.,Jung, H.I.,Jeon, H.,An, Y.J.,Kim, I.K.,Yun, S.,Ahn, H.J.,Chung, K.C.,Lee, S.H.,Suh, P.G.,Kang, S.O.
Crystal structure of filamentous aggregates of human DJ-1 formed in an inorganic phosphate-dependent manner.
J.Biol.Chem., 283:34069-34075, 2008

PubMed Abstract: Mutations in the DJ-1 gene have been implicated in the autosomal recessive early onset parkinsonism. DJ-1 is a soluble dimeric protein with critical roles in response to oxidative stress and in neuronal maintenance. However, several lines of evidence suggest the existence of a nonfunctional aggregated form of DJ-1 in the brain of patients with some neurodegenerative diseases. Here, we show that inorganic phosphate, an important anion that exhibits elevated levels in patients with Parkinson disease, transforms DJ-1 into filamentous aggregates. According to the 2.4-A crystal structure, DJ-1 dimers are linearly stacked through P(i)-mediated interactions to form protofilaments, which are then bundled into a filamentous assembly.

PubMed: 18922803
DOI: 10.1074/jbc.M804243200

Experimental method

X-RAY DIFFRACTION (2.4 Å)