New page: ==Crystal structure of YDR533Cp== <StructureSection load='4qyx' size='340' side='right' caption='4qyx, resolution 1.69Å' scene=''> == Structural highlights == <tab... |
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Structural highlights
Publication Abstract from PubMedThe yeast gene YDR533C encodes a protein belonging to the DJ-1/ThiJ/PfpI superfamily. This family includes the human protein DJ-1, which is mutated in autosomal recessive early-onset Parkinson's disease. The function of DJ-1 and its yeast homologue YDR533Cp is unknown. We report here the crystal structure of YDR533Cp at 1.8-A resolution. The structure indicates that the closest relative to YDR533Cp is the Escherichia coli heat shock protein Hsp31 (YedU), which has both chaperone and protease activity. As expected, the overall fold of the core domain of YDR533Cp is also similar to that of DJ-1 and the bacterial protease PfpI. YDR533Cp contains a possible catalytic triad analogous to that of Hsp31 and an additional domain that is present in Hsp31 but is not seen in DJ-1 and other members of the family. The cysteine in this triad (Cys-138) is oxidized in this crystal structure, similar to modifications seen in the corresponding cysteine in the crystal structure of DJ-1. YDR533Cp appears to be a dimer both in solution and the crystal, but this dimer is formed by a different interface than that found in Hsp31 or other members of the superfamily. The 1.8-A resolution crystal structure of YDR533Cp from Saccharomyces cerevisiae: a member of the DJ-1/ThiJ/PfpI superfamily.,Wilson MA, St Amour CV, Collins JL, Ringe D, Petsko GA Proc Natl Acad Sci U S A. 2004 Feb 10;101(6):1531-6. Epub 2004 Jan 26. PMID:14745011[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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