PDBsum entry 1j42

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RNA binding protein PDB id
Protein chain
185 a.a. *
Waters ×41
* Residue conservation analysis

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Key reference
Title Crystal structures of human dj-1 and escherichia coli hsp31, Which share an evolutionarily conserved domain.
Authors S.J.Lee, S.J.Kim, I.K.Kim, J.Ko, C.S.Jeong, G.H.Kim, C.Park, S.O.Kang, P.G.Suh, H.S.Lee, S.S.Cha.
Ref. J Biol Chem, 2003, 278, 44552-44559. [DOI no: 10.1074/jbc.M304517200]
PubMed id 12939276
Human DJ-1 and Escherichia coli Hsp31 belong to ThiJ/PfpI family, whose members contain a conserved domain. DJ-1 is associated with autosomal recessive early onset parkinsonism and Hsp31 is a molecular chaperone. Structural comparisons between DJ-1, Hsp31, and an Archaea protease, a member of ThiJ/PfpI family, lead to the identification of the chaperone activity of DJ-1 and the proteolytic activity of Hsp31. Moreover, the comparisons provide insights into how the functional diversity is realized in proteins that share an evolutionarily conserved domain. On the basis of the chaperone activity the possible role of DJ-1 in the pathogenesis of Parkinson's disease is discussed.
Figure 1.
FIG. 1. Structure of DJ-1. A, ribbon diagram of a DJ-1 monomer shown with the secondary structures labeled. The core structure is represented by violet. Yellow indicates the insertion into the core structure. The boxed region indicates the dimerization site. The white arrow indicates the location of Leu-166. B, left, ribbon presentation of DJ-1 dimer. An ellipse indicates the location of the hydrophobic patch. Right, molecular surface representation showing the proposed hydrophobic patch. The molecular surface encompassing Val-146, Phe-162, Leu-166, Ala-167, Ala-178, and Leu-187 is colored yellow. The orientation is identical to that of left figure. C, stereo view of the superimposed C tracing of DJ-1 (yellow), Hsp31 (cyan), PH1704 (green), and Cat_ThiJ (pink). The orientation of the molecule is similar to A. The boxed region is the cap domain of Hsp31. A sphere indicates the location of the conserved cysteine residues. D, the 2F[o] - F[c] electron density maps contoured at 1 showing the region around Leu-166.
Figure 7.
FIG. 7. Modification of a cysteine residue into a sulfinic acid under an oxidizing condition. The 2F[o] - F[c] electron density maps contoured at 1 showing Cys-106 of DJ-1. The structure of oxidized DJ-1 was solved at 3.0 Å.
The above figures are reprinted by permission from the ASBMB: J Biol Chem (2003, 278, 44552-44559) copyright 2003.
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