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

Sun Joo Lee, So Jung Kim, In Kwon Kim, Junsang Ko, Chang Sook Jeong, Gyung Hwa Kim, Chankyu Park, Sa Ouk Kang, Pann Ghill Suh, Heung Soo Lee, Sun Shin Cha

Research output: Contribution to journalArticlepeer-review

189 Scopus citations

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.

Original languageEnglish
Pages (from-to)44552-44559
Number of pages8
JournalJournal of Biological Chemistry
Volume278
Issue number45
DOIs
StatePublished - Nov 7 2003

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