CGC Bibliography Paper 5435

NMR structure of conserved eukaryotic protein ZK652.3 from C. elegans: a ubiquitin-like fold.

Cort JR, Chiang Y, Zheng D, Montelione G, Kennedy MA

Medline:

12211038

Citation:

Proteins: Structure, Function, and Genetics 48: 733-736

Type:

ARTICLE

Genes:

Abstract:

Structural proteomics aims to provide one or more representative three-dimensional (3D) structures for every structural domain family in nature. As part of an international effort in structural proteomics, the Northeast Structural Genomics Consortium has targeted clusters of strongly conserved eukaryotic protein families for structural and functional analysis. On this basis, protein ZK652.3 (nes WR41/WP:CE00949/YOY3_CAEEL/ Swiss-Prot P34661/gi17557033) from Caenorhabditis elegans was selected for structure determination. Sequencing of cDNA libraries shows that homologues of ZK6582.3 occur widely in vertebrates and plants (Fig.1). However, ZK652.3 homologues are conspicuously absent from the yeast and Drosophila genomes. Expression of the ZK652.3 gene has been observed in a transcriptional profile of C. elegans, where it was one of a cluster of 89 genes whose expression levels covaried during development. The biochemical function of this protein is presently unknown. Here we describe the 3D structure of ZK652.3 determined by nuclear magnetic resonance (NMR) spectroscopy and discuss structural similarities with other proteins that provide clues to potential biochemical functions.