1IZZ

Crystal structure of Hsp31

Summary for 1IZZ

• Entry DOI: 10.2210/pdb1izz/pdb
• Related: 1IZY
• Descriptor: Hsp31 (2 entities in total)
• Functional Keywords: alpha-beta sandwitch, chaperone, hydrolase
• Biological source: Escherichia coli
• Total number of polymer chains: 1
• Total formula weight: 31228.34

Authors

Cha, S.S.,Lee, S.J. (deposition date: 2002-10-16, release date: 2003-10-16, Last modification date: 2023-12-27)

Primary citation

Lee, S.J.,Kim, S.J.,Kim, I.K.,Ko, J.,Jeong, C.S.,Kim, G.H.,Park, C.,Kang, S.O.,Suh, P.G.,Lee, H.S.,Cha, S.S.
Crystal structures of human DJ-1 and Escherichia coli Hsp31, which share an evolutionarily conserved domain
J.Biol.Chem., 278:44552-44559, 2003

PubMed 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.

PubMed: 12939276
DOI: 10.1074/jbc.M304517200

Experimental method

X-RAY DIFFRACTION (2.31 Å)