1Q2U: Crystal Structure of Dj-1rs and Implication on Familial Parkinson's Disease

DJ-1 is a protein involved in multiple physiological processes, including cancer, Parkinson's disease, and male fertility. It is unknown how DJ-1 functions in the apparently different systems. The crystal structure of DJ-1 at 1.6 A resolution shows that DJ-1 is a helix-strand-helix sandwich and forms a dimer. The DJ-1 structure is similar to the members of the intracellular protease PfpI family. However, the catalytic triad of Cys-His-Glu is not strictly conserved in DJ-1, implying that DJ-1 has a different catalytic mechanism if it acts as a protease or DJ-1 serves as a regulatory protein in the physiological processes. The structure shows that Leu166 positions in the middle of a helix and thus predicts that the L166P mutation will bend the helix and impact the dimerization of DJ-1. As a result, the conformational changes may diminish the DJ-1 binding with its partner, leading to the familial Parkinson's disease caused by the single L166P mutation.
PDB ID: 1Q2UDownload
MMDB ID: 24826
PDB Deposition Date: 2003/7/26
Updated in MMDB: 2012/11 
Experimental Method:
x-ray diffraction
Resolution: 1.6  Å
Source Organism:
Similar Structures:
Biological Unit for 1Q2U: monomeric; determined by author and by software (PQS)
Molecular Components in 1Q2U
Label Count Molecule
Protein (1 molecule)
RNA-binding Protein Regulatory Subunit
Molecule annotation
* Click molecule labels to explore molecular sequence information.

Citing MMDB