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 responsible for the access of
different peptide substrates.
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Document Type: Research Article
Hefei National Laboratory for Physical Sciences at Microscale and School of Life Sciences, University of Science and Technology of China, Hefei, Anhui 230027, People's Republic of China
Publication date: December 1, 2010