BAIT

HSP33

YOR391C
Possible chaperone and cysteine protease; required for transcriptional reprogramming during the diauxic shift and for survival in stationary phase; similar to E. coli Hsp31 and S. cerevisiae Hsp31p, Hsp32p, and Sno4p; member of the DJ-1/ThiJ/PfpI superfamily, which includes human DJ-1 involved in Parkinson's disease and cancer
GO Process (1)
GO Function (2)
GO Component (0)

Gene Ontology Biological Process

Saccharomyces cerevisiae (S288c)
PREY

HSP33

YOR391C
Possible chaperone and cysteine protease; required for transcriptional reprogramming during the diauxic shift and for survival in stationary phase; similar to E. coli Hsp31 and S. cerevisiae Hsp31p, Hsp32p, and Sno4p; member of the DJ-1/ThiJ/PfpI superfamily, which includes human DJ-1 involved in Parkinson's disease and cancer
GO Process (1)
GO Function (2)
GO Component (0)

Gene Ontology Biological Process

Saccharomyces cerevisiae (S288c)

Co-crystal Structure

Interaction directly demonstrated at the atomic level by X-ray crystallography. Also used for NMR or Electron Microscopy (EM) structures. If there is no obvious bait-hit directionality to the interaction involving 3 or more proteins, then the co-crystallized proteins should be listed as a complex.

Publication

Structure of Hsp33/YOR391Cp from the yeast Saccharomyces cerevisiae.

Guo PC, Zhou YY, Ma XX, Li WF

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 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 ... [more]

Acta Crystallogr. Sect. F Struct. Biol. Cryst. Commun. Dec. 01, 2010; 66(0);1557-61 [Pubmed: 21139195]

Throughput

  • Low Throughput

Curated By

  • BioGRID