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PDBsum entry 1pdv

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Protein binding PDB id
1pdv
Jmol
Contents
Protein chain
187 a.a. *
Waters ×192
* Residue conservation analysis

References listed in PDB file
Key reference
Title Crystal structure of human dj-1, A protein associated with early onset parkinson'S disease.
Authors X.Tao, L.Tong.
Ref. J Biol Chem, 2003, 278, 31372-31379. [DOI no: 10.1074/jbc.M304221200]
PubMed id 12761214
Abstract
We report the crystal structure at 1.8-A resolution of human DJ-1, which has been linked to early onset Parkinson's disease. The monomer of DJ-1 contains the alpha/beta-fold that is conserved among members of the DJ-1/ThiJ/PfpI superfamily. However, the structure also contains an extra helix at the C terminus, which mediates a novel mode of dimerization for the DJ-1 proteins. A putative active site has been identified near the dimer interface, and the residues Cys-106, His-126, and Glu-18 may play important roles in the catalysis by this protein. Studies with the disease-causing L166P mutant suggest that the mutation has disrupted the C-terminal region and the dimerization of the protein. The DJ-1 proteins may function only as dimers. The Lys to Arg mutation at residue 130, the site of sumoylation of DJ-1, has minimal impact on the structure of the protein.
Figure 4.
FIG. 4. The putative active site of DJ-1. A, schematic drawing of the structure near the Cys-106 residue of DJ-1. The two monomers are colored in green and cyan, respectively. B, molecular surface of the DJ-1 dimer near the putative active site. Panel A was produced with Ribbons (39), and panel B was produced with Grasp (40).
Figure 6.
FIG. 6. The environment of the Leu-166 residue. Stereo drawing showing the hydrophobic core among helices A, G, and H. The side chain of Leu-166 is shown in red. Residues Ile-168 and Leu-172 belong to the hydrophobic core with the central -sheet of the structure. This figure was produced with Ribbons (39).
The above figures are reprinted by permission from the ASBMB: J Biol Chem (2003, 278, 31372-31379) copyright 2003.
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