Structural highlights
Function
HSP33_YEAST Probable protease. May act as a chaperone (By similarity).
Publication Abstract from PubMed
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 alpha2-alpha3 of the core domain might be responsible for the access of different peptide substrates.
Structure of Hsp33/YOR391Cp from the yeast Saccharomyces cerevisiae.,Guo PC, Zhou YY, Ma XX, Li WF Acta Crystallogr Sect F Struct Biol Cryst Commun. 2010 Dec 1;66(Pt, 12):1557-61. Epub 2010 Nov 16. PMID:21139195[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Guo PC, Zhou YY, Ma XX, Li WF. Structure of Hsp33/YOR391Cp from the yeast Saccharomyces cerevisiae. Acta Crystallogr Sect F Struct Biol Cryst Commun. 2010 Dec 1;66(Pt, 12):1557-61. Epub 2010 Nov 16. PMID:21139195 doi:10.1107/S1744309110039965
