Crystal structure of the YDR533c S. cerevisiae protein, a class II member of the Hsp31 family

Structure. 2004 May;12(5):839-47. doi: 10.1016/j.str.2004.02.030.


The ORF YDR533c from Saccharomyces cerevisiae codes for a 25.5 kDa protein of unknown biochemical function. Transcriptome analysis of yeast has shown that this gene is activated in response to various stress conditions together with proteins belonging to the heat shock family. In order to clarify its biochemical function, we determined the crystal structure of YDR533c to 1.85 A resolution by the single anomalous diffraction method. The protein possesses an alpha/beta hydrolase fold and a putative Cys-His-Glu catalytic triad common to a large enzyme family containing proteases, amidotransferases, lipases, and esterases. The protein has strong structural resemblance with the E. coli Hsp31 protein and the intracellular protease I from Pyrococcus horikoshii, which are considered class I and class III members of the Hsp31 family, respectively. Detailed structural analysis strongly suggests that the YDR533c protein crystal structure is the first one of a class II member of the Hsp31 family.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amino Acid Sequence
  • Catalytic Domain
  • Dimerization
  • Heat-Shock Proteins / chemistry*
  • Heat-Shock Proteins / genetics
  • Molecular Sequence Data
  • Multigene Family
  • Protein Structure, Tertiary
  • Saccharomyces cerevisiae / chemistry*
  • Saccharomyces cerevisiae / genetics
  • Saccharomyces cerevisiae Proteins / chemistry*
  • Saccharomyces cerevisiae Proteins / genetics


  • Heat-Shock Proteins
  • Saccharomyces cerevisiae Proteins
  • HSP31 protein, S cerevisiae

Associated data

  • PDB/1QVV
  • PDB/1QVW
  • PDB/1QVZ