Crystal Structures of Human DJ-1 and Escherichia coli Hsp31, Which Share an Evolutionarily Conserved Domain

• Published in: The Journal of biological chemistry Vol. 278; no. 45; pp. 44552 - 44559
• Main Authors: Lee, Sun-Joo, Kim, So Jung, Kim, In-Kwon, Ko, Junsang, Jeong, Chang-Sook, Kim, Gyung-Hwa, Park, Chankyu, Kang, Sa-Ouk, Suh, Pann-Ghill, Lee, Heung-Soo, Cha, Sun-Shin
• Format: Journal Article
• Language: English
• Published: United States Elsevier Inc 07.11.2003; American Society for Biochemistry and Molecular Biology
• Subjects: Amino Acid Sequence; Binding Sites; Chemical Phenomena; Chemistry, Physical; Computer Simulation; Conserved Sequence; Crystallization; Dimerization; DJ-1 protein; Escherichia coli; Escherichia coli Proteins - chemistry; Escherichia coli Proteins - genetics; Escherichia coli Proteins - metabolism; Gene Deletion; Hsp31 protein; Humans; Intracellular Signaling Peptides and Proteins; Luciferases - metabolism; Models, Molecular; Molecular Chaperones - chemistry; Molecular Chaperones - genetics; Molecular Chaperones - metabolism; Molecular Sequence Data; Molecular Structure; Mutagenesis; Nerve Tissue Proteins - genetics; Oncogene Proteins - chemistry; Oncogene Proteins - genetics; Oncogene Proteins - metabolism; Oxidation-Reduction; Parkinson Disease - genetics; Peptide Fragments - genetics; Peptide Hydrolases - metabolism; Point Mutation; Protein Deglycase DJ-1; Protein Structure, Quaternary; Synucleins; Ubiquitin-Protein Ligases - genetics
• ISSN: 0021-9258; 1083-351X
• DOI: 10.1074/jbc.M304517200

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.