title: Crystal structures of human DJ-1 and Escherichia coli Hsp31, which share an evolutionarily conserved domain.
abstract: 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.
authors.affiliation: Beamline Division, Pohang Accelerator Laboratory, Pohang, 790-784, Kyungbuk, Republic of Korea.
authors.forename: Sun-Joo
authors.initials: SJ
authors.lastname: Lee
authors.forename: So Jung
authors.initials: SJ
authors.lastname: Kim
authors.forename: In-Kwon
authors.initials: IK
authors.lastname: Kim
authors.forename: Junsang
authors.initials: J
authors.lastname: Ko
authors.forename: Chang-Sook
authors.initials: CS
authors.lastname: Jeong
authors.forename: Gyung-Hwa
authors.initials: GH
authors.lastname: Kim
authors.forename: Chankyu
authors.initials: C
authors.lastname: Park
authors.forename: Sa-Ouk
authors.initials: SO
authors.lastname: Kang
authors.forename: Pann-Ghill
authors.initials: PG
authors.lastname: Suh
authors.forename: Heung-Soo
authors.initials: HS
authors.lastname: Lee
authors.forename: Sun-Shin
authors.initials: SS
authors.lastname: Cha
mesh_terms: D000595:Amino Acid Sequence; D001665:Binding Sites; D055598:Chemical Phenomena; D002627:Chemistry, Physical; D003198:Computer Simulation; D017124:Conserved Sequence; D003460:Crystallization; D019281:Dimerization; D029968:Escherichia coli Proteins / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism; D017353:Gene Deletion; D006801:Humans; D047908:Intracellular Signaling Peptides and Proteins; D008156:Luciferases / Q000378:metabolism; D008958:Models, Molecular; D018832:Molecular Chaperones / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism; D008969:Molecular Sequence Data; D015394:Molecular Structure; D016296:Mutagenesis; D009419:Nerve Tissue Proteins / Q000235:genetics; D015513:Oncogene Proteins / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism; D010084:Oxidation-Reduction; D010300:Parkinson Disease / Q000235:genetics; D010446:Peptide Fragments / Q000235:genetics; D010447:Peptide Hydrolases / Q000378:metabolism; D017354:Point Mutation; D000071617:Protein Deglycase DJ-1; D020836:Protein Structure, Quaternary; D051843:Synucleins; D044767:Ubiquitin-Protein Ligases / Q000235:genetics
chemical_list: D029968:Escherichia coli Proteins; D047908:Intracellular Signaling Peptides and Proteins; D018832:Molecular Chaperones; D009419:Nerve Tissue Proteins; D015513:Oncogene Proteins; D010446:Peptide Fragments; D051843:Synucleins; C469996:hchA protein, E coli; D008156:Luciferases; D044767:Ubiquitin-Protein Ligases; C111567:parkin protein; C105131:PARK7 protein, human; D000071617:Protein Deglycase DJ-1; D010447:Peptide Hydrolases