1IZY

Crystal structure of Hsp31

1IZY の概要

• エントリーDOI: 10.2210/pdb1izy/pdb
• 関連するPDBエントリー: 1IZZ
• 分子名称: Hsp31 (1 entity in total)
• 機能のキーワード: alpha-beta sandwitch, chaperone, hydrolase
• 由来する生物種: Escherichia coli
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 62432.79

構造登録者

Cha, S.S.,Lee, S.J. (登録日: 2002-10-16, 公開日: 2003-10-16, 最終更新日: 2023-12-27)

主引用文献

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

実験手法

X-RAY DIFFRACTION (2.8 Å)