3MII

Crystal structure of Y0R391Cp/HSP33 from Saccharomyces cerevisiae

Summary for 3MII

• Entry DOI: 10.2210/pdb3mii/pdb
• Related: 1QVV 3KKL
• Descriptor: Probable chaperone protein HSP33, TRIETHYLENE GLYCOL, GLYCEROL, ... (5 entities in total)
• Functional Keywords: heat shock protein, hydrolase
• Biological source: Saccharomyces cerevisiae (Baker's yeast)
• Total number of polymer chains: 2
• Total formula weight: 54473.60

Authors

Guo, P.-C.,Zhou, Y.-Y.,Zhou, C.-Z.,Li, W.-F. (deposition date: 2010-04-10, release date: 2010-12-08, Last modification date: 2024-11-06)

Primary citation

Guo, P.-C.,Zhou, Y.-Y.,Ma, X.-X.,Li, W.-F.
Structure of Hsp33/YOR391Cp from the yeast Saccharomyces cerevisiae
Acta Crystallogr.,Sect.F, 66:1557-1561, 2010

PubMed 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.

PubMed: 21139195
DOI: 10.1107/S1744309110039965

Experimental method

X-RAY DIFFRACTION (2.4 Å)