1qvv
Crystal structure of the S. cerevisiae YDR533c proteinCrystal structure of the S. cerevisiae YDR533c protein
Structural highlights
FunctionHSP31_YEAST Probable protease. May act as a chaperone. Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedThe 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. Crystal structure of the YDR533c S. cerevisiae protein, a class II member of the Hsp31 family.,Graille M, Quevillon-Cheruel S, Leulliot N, Zhou CZ, de la Sierra Gallay IL, Jacquamet L, Ferrer JL, Liger D, Poupon A, Janin J, van Tilbeurgh H Structure. 2004 May;12(5):839-47. PMID:15130476[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
|
| ||||||||||||||||||