Journal
ACTA CRYSTALLOGRAPHICA SECTION F-STRUCTURAL BIOLOGY COMMUNICATIONS
Volume 66, Issue -, Pages 1557-1561Publisher
INT UNION CRYSTALLOGRAPHY
DOI: 10.1107/S1744309110039965
Keywords
Hsp33; YOR391Cp; Saccharomyces cerevisiae; ThiI; DJ-1; PfpI superfamily
Funding
- Ministry of Science and Technology of China [2006CB910202, 2006CB806501]
- Chinese National Natural Science Foundation [30870490]
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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 A resolution. Structural comparison revealed that Hsp33 adopts an alpha/beta-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 alpha 2-alpha 3 of the core domain might be responsible for the access of different peptide substrates.
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