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Structure of Hsp33/YOR391Cp from the yeast Saccharomyces cerevisiae.

ABSTRACT: Saccharomyces cerevisiae Hsp33/YOR391Cp is a member of the ThiI/DJ-1/PfpI superfamily. Hsp33 was overexpressed in Escherichia coli and its crystal structure was determined at 2.40?Å resolution. Structural comparison revealed that Hsp33 adopts an ?/?-hydrolase fold and possesses the putative Cys-His-Glu catalytic triad common to the Hsp31 family, suggesting that Hsp33 and Hsp31 share similar aminopeptidase activity, while structural deviations in helices ?2-?3 of the core domain might be responsible for the access of different peptide substrates.

SUBMITTER: Guo PC

PROVIDER: S-EPMC2998354 | biostudies-literature | 2010 Dec

REPOSITORIES: biostudies-literature

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Structure of Hsp33/YOR391Cp from the yeast Saccharomyces cerevisiae.

Guo Peng Chao PC Zhou Ye Yun YY Ma Xiao Xiao XX Li Wei Fang WF

Acta crystallographica. Section F, Structural biology and crystallization communications 20101116 Pt 12

Saccharomyces cerevisiae Hsp33/YOR391Cp is a member of the ThiI/DJ-1/PfpI superfamily. Hsp33 was overexpressed in Escherichia coli and its crystal structure was determined at 2.40 Å resolution. Structural comparison revealed that Hsp33 adopts an α/β-hydrolase fold and possesses the putative Cys-His-Glu catalytic triad common to the Hsp31 family, suggesting that Hsp33 and Hsp31 share similar aminopeptidase activity, while structural deviations in helices α2-α3 of the core domain might be responsi ...[more]

PMID: 21139195

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