1rw7

From Proteopedia

Crystal Structure of YDR533Cp

Overview

The 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.

About this Structure

1RW7 is a Single protein structure of sequence from Saccharomyces cerevisiae. Full crystallographic information is available from OCA.

Reference

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

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