Structure of Hsp33/YOR391Cp from the yeast Saccharomyces cerevisiae.
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.
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.
Peng Chao
PC
Guo
Ye Yun
YY
Zhou
Xiao Xiao
XX
Ma
Wei Fang
WF
Li
D000595:Amino Acid Sequence; D000626:Aminopeptidases / Q000737:chemistry*; D020134:Catalytic Domain; D018360:Crystallography, X-Ray; D006360:Heat-Shock Proteins / Q000737:chemistry; D008958:Models, Molecular; D008969:Molecular Sequence Data; D055503:Protein Multimerization; D017433:Protein Structure, Secondary; D012441:Saccharomyces cerevisiae / Q000737:chemistry*; D029701:Saccharomyces cerevisiae Proteins / Q000737:chemistry*; D016415:Sequence Alignment; D040681:Structural Homology, Protein
D006360:Heat-Shock Proteins; D029701:Saccharomyces cerevisiae Proteins; D000626:Aminopeptidases; C556680:Hsp33 protein, S cerevisiae; C496117:HSP31 protein, S cerevisiae