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Structure of Hsp33/YOR391Cp from the yeast Saccharomyces cerevisiae.

Authors :
Guo, Peng-Chao
Zhou, Ye-Yun
Ma, Xiao-Xiao
Li, Wei-Fang
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