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Structure of Hsp33/YOR391Cp from the yeast Saccharomyces cerevisiae.
- Source :
-
Acta Crystallographica: Section F (Wiley-Blackwell) . Dec2010, Vol. 66 Issue 12, p1557-1561. 5p. - Publication Year :
- 2010
-
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 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. [ABSTRACT FROM AUTHOR]
Details
- Language :
- English
- ISSN :
- 17443091
- Volume :
- 66
- Issue :
- 12
- Database :
- Academic Search Index
- Journal :
- Acta Crystallographica: Section F (Wiley-Blackwell)
- Publication Type :
- Academic Journal
- Accession number :
- 110812635
- Full Text :
- https://doi.org/10.1107/S1744309110039965