1QVZ

Crystal structure of the S. cerevisiae YDR533c protein

Summary for 1QVZ

• Entry DOI: 10.2210/pdb1qvz/pdb
• Related: 1QVV 1QVW
• Descriptor: YDR533c protein (2 entities in total)
• Functional Keywords: alpha/beta hydrolase fold, catalytic triad, heat shock protein, structural genomics, unknown function
• Biological source: Saccharomyces cerevisiae (baker's yeast)
• Total number of polymer chains: 2
• Total formula weight: 51971.20

Authors

Graille, M.,Leulliot, N.,Quevillon-Cheruel, S.,van Tilbeurgh, H. (deposition date: 2003-08-29, release date: 2004-03-30, Last modification date: 2024-10-09)

Primary citation

Graille, M.,Quevillon-Cheruel, S.,Leulliot, N.,Zhou, C.Z.,de la Sierra Gallay, I.L.,Jacquamet, L.,Ferrer, J.L.,Liger, D.,Poupon, A.,Janin, J.,van Tilbeurgh, H.
Crystal structure of the YDR533c S. cerevisiae protein, a class II member of the Hsp31 family
STRUCTURE, 12:839-847, 2004

PubMed Abstract: 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.

PubMed: 15130476
DOI: 10.1016/j.str.2004.02.030

Experimental method

X-RAY DIFFRACTION (1.85 Å)